Omneity® Pellets
All-In-One Vitamin & Mineral Pellet
Biochemistry.
Periodical
Biochemistry
Publisher:
American Chemical Society.
Frequency: Weekly,
Country: United States
Language: English
Author(s):
American Chemical Society.
Start Year:1962 -
ISSN:
0006-2960 (Print)
1520-4995 (Electronic)
0006-2960 (Linking)
1520-4995 (Electronic)
0006-2960 (Linking)
Impact Factor
2.9
2022
| NLM ID: | 0370623 |
| (DNLM): | B15160000(s) |
| (OCoLC): | 01536396 |
| Coden: | BICHAW |
| Classification: | W1 BI635 |
Physical properties and subunit structure of butyrylcholinesterase from horse serum.
Biochemistry
April 10, 1973
Volume 12, Issue 8 1622-1630 doi: 10.1021/bi00732a025
Lee JC, Harpst JA.No abstract available Equilibria of organic phosphates with horse oxyhemoglobin.
Biochemistry
December 5, 1972
Volume 11, Issue 25 4660-4668 doi: 10.1021/bi00775a004
Hedlund B, Danielson C, Lovrien R.Organic phosphates, ATP, AMP, and 2,3-di-phosphoglycerate (DPG) were interacted with horse oxyhemo-globin. Binding parameters were obtained by means of dialysis equilibrium in buffers at 5°, and from calorimetry at 5 and 25°, all in the pH mom 6.5-7.3. The calorimetric results were evaluated assuming a single strong site, and assuming that the pH shifts which occur in the absence of added salt are due to electrostatic effects and not to changes in side-chain titration, upon mixing samples previously ad-justed to the same pH. There was obtained for ATP and 2,3- diphosphoglycerate. respectivel... Spectroscopic properties of N-bromosuccinimide-modified horse heart cytochrome c + .
Biochemistry
November 7, 1972
Volume 11, Issue 23 4209-4216 doi: 10.1021/bi00773a003
Myer YP, Pal PK.No abstract available Mechanistic studies on horse liver alcohol dehydrogenase. The influence of the different premixings on the transient kinetics of aldehyde reductions.
Biochemistry
June 6, 1972
Volume 11, Issue 12 2303-2310 doi: 10.1021/bi00762a015
Luisi PL, Favilla R.No abstract available Electronic, hydrophobic, and steric effects of binding of inhibitors to the horse liver alcohol dehydrogenase-reduced pyridine coenzyme binary complex.
Biochemistry
January 18, 1972
Volume 11, Issue 2 170-179 doi: 10.1021/bi00752a006
Sarma RH, Woronick CL.No abstract available Equine antihapten antibody. Studies on the primary structure and conformation of equine immunoglobulins.
Biochemistry
October 27, 1970
Volume 9, Issue 22 4310-4321 doi: 10.1021/bi00824a011
Rockey JH, Montgomery PC, Dorrington KJ.No abstract available Zinc isotope exchange in horse liver alcohol dehydrogenase.
Biochemistry
September 1, 1969
Volume 8, Issue 9 3792-3797 doi: 10.1021/bi00837a045
Drum DE, Li TK, Vallee BL.No abstract available Equine antihapten antibody. The molecular weights of the subunits of equine immunoglobulins.
Biochemistry
March 1, 1969
Volume 8, Issue 3 1247-1258 doi: 10.1021/bi00831a060
Montgomery PC, Dorrington KJ, Rockey JH.Three independent methods have been used
to determine the molecular weights of the heavyand light-polypeptide chain subunits of equine yGab-,
yGc-, and yT-immunoglobulins. Extensively reduced
and alkylated proteins were filtered through standard
columns of Sephadex G-100 or G-200 in 8 M urea405
M propionic acid. Subunit molecular weights were obtained from the linear elution volume, V,, us. logarithm
molecular weight relationship defined for each column
with rabbit yG-globulin heavy and light chains and
horse heart cytochrome c. Molecular weights also were
determined by equilibrium se... Equine antihapten antibody. VI. Subunits of polyalanylated gamma-G(T)-immunoglobulin.
Biochemistry
July 1, 1968
Volume 7, Issue 7 2462-2468 doi: 10.1021/bi00847a003
Genco RJ, Karush F, Tenenhouse HS.No abstract available Horse Heart Cytochrome C: Spectrophotometric Titration and Viscosity Changes in Alkaline Solution.
Biochemistry
November 1, 1964
Volume 3 1648-1650 doi: 10.1021/bi00899a008
RUPLEY JA.No abstract available The Specific Polysaccharide of Type XVIII Pneumococcus. III.
Biochemistry
November 1, 1963
Volume 2 1288-1294 doi: 10.1021/bi00906a020
ESTRADA-PARRA S, HEIDELBERGER M.No abstract available Methylation of histidine-48 in pancreatic phospholipase A2. Role of histidine and calcium ion in the catalytic mechanism.
Biochemistry
February 19, 1980
Volume 19, Issue 4 743-750 doi: 10.1021/bi00545a021
Verheij HM, Volwerk JJ, Jansen EH, Puyk WC, Dijkstra BW, Drenth J, de Haas GH.It is known that His-48 is part of the active center in pancreatic phospholipase. To further elucidate the role of histidine-48 in the active center of pancreatic phospholipase A2, we have modified the enzyme with a number of bromo ketones and methyl benzenesulfonates. Rapid methylation occurred with methyl p-nitrobenzenesulfonate. Methylated phospholipase shows total loss of enzymatic activity whereas binding of substrate and the cofactor Ca2+ remains intact. Amino acid analysis of methylated equine phospholipase showed the loss of the single molecule of histidine and the formation of one mol... Read More
34
Structure of glycan moieties responsible for the extended circulatory life time of fetal bovine serum acetylcholinesterase and equine serum butyrylcholinesterase.
Biochemistry
June 17, 1997
Volume 36, Issue 24 7481-7489 doi: 10.1021/bi963156d
Saxena A, Raveh L, Ashani Y, Doctor BP.Cholinesterases are serine hydrolases that can potentially be used as pretreatment drugs for organophosphate toxicity, as drugs to alleviate succinylcholine-induced apnea, and as detoxification agents for environmental toxins such as heroin and cocaine. The successful application of serum-derived cholinesterases as bioscavengers stems from their relatively long residence time in the circulation. To better understand the relationship between carbohydrate structure and the stability of cholinesterases in circulation, we determined the monosaccharide composition, the distribution of various oligo... Read More
19
Characterization of human, bovine, and horse antithrombin III.
Biochemistry
January 27, 1976
Volume 15, Issue 2 368-373 doi: 10.1021/bi00647a020
Kurachi K, Schmer G, Hermodson MA, Teller DC, Davie EW.A comparison of the physical-chemical properties of human, bovine, and horse antithrombin III has been made. These three plasma proteins are strong inhibitors of bovine factor Xa and form a 1:1 molar complex with this coagulation enzyme. Human, bovine, and horse antithrombin III are glycoproteins containing hexose, hexosamine, and neuraminic acid. The total carbohydrate was 9, 12, and 16% for human, bovine, and horse antithrombin III, respectively. These proteins have a similar amino acid composition, although some monor variations were noted. Each antithrombin III is composed of a single poly... Read More
18
Characterization of hydrophobic cores in apomyoglobin: a proton NMR spectroscopy study.
Biochemistry
December 18, 1990
Volume 29, Issue 50 11067-11072 doi: 10.1021/bi00502a008
Cocco MJ, Lecomte JT.A proton nuclear magnetic resonance spectroscopic study of horse apomyoglobin was undertaken in order to define the regions of myoglobin that are and that are not structurally affected by the binding of the prosthetic group. It was found that, in spite of the poor spectral resolution, a number of spin systems could be identified by using standard correlated methods. Four clusters consisting mostly of hydrophobic residues were detected by nuclear Overhauser spectroscopy, two of which involved the tryptophan side chains. Extensive similarities to nuclear Overhauser spectroscopy data collected on... Read More
17
Deprotonation of the horse liver alcohol dehydrogenase-NAD+ complex controls formation of the ternary complexes.
Biochemistry
September 21, 2005
Volume 44, Issue 38 12797-12808 doi: 10.1021/bi050865v
Kovaleva EG, Plapp BV.Binding of NAD+ to wild-type horse liver alcohol dehydrogenase is strongly pH-dependent and is limited by a unimolecular step, which may be related to a conformational change of the enzyme-NAD+ complex. Deprotonation during binding of NAD+ and inhibitors that trap the enzyme-NAD+ complex was examined by transient kinetics with pH indicators, and formation of complexes was monitored by absorbance and protein fluorescence. Reactions with pyrazole and trifluoroethanol had biphasic proton release, whereas reaction with caprate showed proton release followed by proton uptake. Proton release (200-55... Read More
17
Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis.
Biochemistry
July 7, 2017
Volume 56, Issue 28 3632-3646 doi: 10.1021/acs.biochem.7b00446
Plapp BV, Savarimuthu BR, Ferraro DJ, Rubach JK, Brown EN, Ramaswamy S.During catalysis by liver alcohol dehydrogenase (ADH), a water bound to the catalytic zinc is replaced by the oxygen of the substrates. The mechanism might involve a pentacoordinated zinc or a double-displacement reaction with participation by a nearby glutamate residue, as suggested by studies of human ADH3, yeast ADH1, and some other tetrameric ADHs. Zinc coordination and participation of water in the enzyme mechanism were investigated by X-ray crystallography. The apoenzyme and its complex with adenosine 5'-diphosphoribose have an open protein conformation with the catalytic zinc in one pos... Read More
17
A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin.
Biochemistry
August 27, 2003
Volume 42, Issue 34 10113-10125 doi: 10.1021/bi030059t
Robinson VL, Smith BB, Arnone A.In 1947, Perutz and co-workers reported that crystalline horse methemoglobin undergoes a large lattice transition as the pH is decreased from 7.1 to 5.4. We have determined the pH 7.1 and 5.4 crystal structures of horse methemoglobin at 1.6 and 2.1 A resolution, respectively, and find that this lattice transition involves a 23 A translation of adjacent hemoglobin tetramers as well as changes in alpha heme ligation and the tertiary structure of the alpha subunits. Specifically, when the pH is lowered from 7.1 to 5.4, the Fe(3+) alpha heme groups (but not the beta heme groups) are converted from... Read More
17
The proximal ligand variant His93Tyr of horse heart myoglobin.
Biochemistry
February 14, 1995
Volume 34, Issue 6 1997-2005 doi: 10.1021/bi00006a021
Hildebrand DP, Burk DL, Maurus R, Ferrer JC, Brayer GD, Mauk AG.The spectroscopic and structural properties of the His93Tyr variant of horse heart myoglobin have been studied to assess the effects of replacing the proximal His residue of this protein with a tyrosyl residue as occurs in catalases from various sources. The variant in the ferric form exhibits electronic spectra that are independent of pH between pH 7 and 10, and it exhibits changes in absorption maxima and intensity that are consistent with a five-coordinate heme iron center at the active site. The EPR spectrum of the variant is that of a high-spin, rhombic system similar to that reported for... Read More
16
Unfolding pathway of myoglobin. Evidence for a multistate process.
Biochemistry
August 30, 1983
Volume 22, Issue 18 4165-4170 doi: 10.1021/bi00287a001
Bismuto E, Colonna G, Irace G.The free energy of unfolding of horse myoglobin has been calculated from the denaturation pattern induced by guanidine hydrochloride as well as by acid. The delta GH2O, i.e., the value in the absence of denaturant obtained by using the two-state transition model, was found to be 25% lower than that determined from the acid denaturation pattern, i.e., 12.0 kcal/mol, although the extent of protein denaturation produced by acid was much lower. The amount of helical structure surviving the acid-induced conformational change was estimated to be 50% of that present in the native protein, and it coul... Read More
13
Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C.
Biochemistry
January 23, 2002
Volume 41, Issue 4 1372-1380 doi: 10.1021/bi011371a
Hagen SJ, Latypov RF, Dolgikh DA, Roder H.Time-resolved spectroscopic studies of unfolded horse iron(II) cytochrome c have suggested that the imidazole side chains of His26 and His33 bind transiently to the heme iron on microsecond time scales, after photodissociation of a carbon monoxide ligand from the heme. Our studies of four variants of cytochrome c (horse wild type, horse H33N, horse H33N/H26Q, and tuna wild type), unfolded in guanidine hydrochloride at pH 6.5, demonstrate that these side chains are responsible for the observed microsecond spectral changes. As His33 and then His26 are eliminated from the horse wild-type sequence... Read More
12
Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Thr42, and Thr46.
Biochemistry
June 4, 1996
Volume 35, Issue 22 7077-7083 doi: 10.1021/bi952900b
Taddei N, Stefani M, Magherini F, Chiti F, Modesti A, Raugei G, Ramponi G.Asn41, Thr42, and Thr46 are invariant residues in both muscle and erythrocyte acylphosphatases isolated so far. Horse muscle acylphosphatase solution structure suggests their close spatial relationship to Arg23, the main substrate binding site. The catalytic and structural role of such residues, as well as their influence on muscle acylphosphatase stability, was investigated by preparing several gene mutants (Thr42Ala, Thr46Ala, Asn41Ala, Asn41Ser, and Asn41Gln) by oligonucleotide-directed mutagenesis. The mutated genes were cloned and expressed in Escherichia coli, and the mutant enzymes were... Read More
11
Partially folded states of equine lysozyme. Structural characterization and significance for protein folding.
Biochemistry
November 9, 1993
Volume 32, Issue 44 11886-11894 doi: 10.1021/bi00095a018
Van Dael H, Haezebrouck P, Morozova L, Arico-Muendel C, Dobson CM.Despite their homologous structure, c-type lysozymes and alpha-lactalbumins have been found to differ profoundly in their unfolding behavior, in that the alpha-lactalbumins readily enter a partially unfolded collapsed state (the "molten globule"), whereas lysozymes unfold cooperatively to a highly unfolded state. The calcium-binding property of lysozyme from equine milk provides an evolutionary link between the two families of proteins. We demonstrate here that equine lysozyme undergoes a two-stage unfolding transition upon heating or in the presence of guanidine hydrochloride that is highly d... Read More
11
Substrate specificities of tissue kallikrein and T-kininogenase: their possible role in kininogen processing.
Biochemistry
June 2, 1992
Volume 31, Issue 21 4969-4974 doi: 10.1021/bi00136a008
Chagas JR, Hirata IY, Juliano MA, Xiong W, Wang C, Chao J, Juliano L, Prado ES.The present studies demonstrate the importance of subsite interactions in determining the cleavage specificities of kallikrein gene family proteinases. The effect of substrate amino acid residues in positions P3-P'3 on the catalytic efficiency of tissue kallikreins (rat, pig, and horse) and T-kininogenase was studied using peptidyl-pNA and intramolecularly quenched fluorogenic peptides as substrates. Kinetic analyses show the different effects of D-amino acid residues at P3, Pro at P'2, and Arg at either P'1 or P'3 on the hydrolysis of substrates by tissue kallikreins from rat and from horse o... Read More
11
Mössbauer spectroscopic study of the initial stages of iron-core formation in horse spleen apoferritin: evidence for both isolated Fe(III) atoms and oxo-bridged Fe(III) dimers as early intermediates.
Biochemistry
June 27, 1989
Volume 28, Issue 13 5486-5493 doi: 10.1021/bi00439a025
Bauminger ER, Harrison PM, Nowik I, Treffry A.Ferritin stores iron within a hollow protein shell as a polynuclear Fe(III) hydrous oxide core. Although iron uptake into ferritin has been studied previously, the early stages in the creation of the core need to be clarified. These are dealt with in this paper by using Mössbauer spectroscopy, a technique that enables several types of Fe(II) and Fe(III) to be distinguished. Systematic Mössbauer studies were performed on samples prepared by adding 57Fe(II) atoms to apoferritin as a function of pH (5.6-7.0), n [the number of Fe/molecule (4-480)], and tf (the time the samples were held at room ... Read More
11
Conformational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochromes-c by weak salt denaturants.
Biochemistry
February 13, 2003
Volume 42, Issue 6 1684-1695 doi: 10.1021/bi0271042
Qureshi SH, Moza B, Yadav S, Ahmad F.The denaturation of bovine and horse cytochromes-c by weak salt denaturants (LiCl and CaCl(2)) was measured at 25 degrees C by observing changes in molar absorbance at 400 nm (Delta epsilon(400)) and circular dichroism (CD) at 222 and 409 nm. Measurements of Delta epsilon(400) and mean residue ellipticity at 409 nm ([theta](409)) gave a biphasic transition for both modes of denaturation of cytochromes-c. It has been observed that the first denaturation phase, N (native) conformation X (intermediate) conformation and the second denaturation phase, X conformation D (denatured) conformation are... Read More
10
Studies on the substrate specificity of the proteinase of equine infectious anemia virus using oligopeptide substrates.
Biochemistry
April 6, 1993
Volume 32, Issue 13 3347-3353 doi: 10.1021/bi00064a018
Tözsér J, Friedman D, Weber IT, Bláha I, Oroszlan S.The proteinase of the equine infectious anemia virus (EIAV), a lentivirus closely related to human immunodeficiency virus (HIV), was purified from concentrated virus. The specificity of the enzyme was characterized using oligopeptides representing naturally occurring cleavage sites in the Gag and Gag-Pol polyproteins. The length of the substrate binding pocket was found to be 1-2 residues longer than that of HIV proteinases. Although the EIAV and HIV proteinases cleaved most of the peptides at the same bond, some were hydrolyzed by only the EIAV enzyme. Oligopeptides representing cleavage site... Read More
10
Equine antihapten antibody. The molecular weights of the subunits of equine immunoglobulins.
Biochemistry
March 1, 1969
Volume 8, Issue 3 1247-1258 doi: 10.1021/bi00831a060
Montgomery PC, Dorrington KJ, Rockey JH.Three independent methods have been used
to determine the molecular weights of the heavyand light-polypeptide chain subunits of equine yGab-,
yGc-, and yT-immunoglobulins. Extensively reduced
and alkylated proteins were filtered through standard
columns of Sephadex G-100 or G-200 in 8 M urea405
M propionic acid. Subunit molecular weights were obtained from the linear elution volume, V,, us. logarithm
molecular weight relationship defined for each column
with rabbit yG-globulin heavy and light chains and
horse heart cytochrome c. Molecular weights also were
determined by equilibrium se... Mechanism of binding of horse liver alcohol dehydrogenase and nicotinamide adenine dinucleotide.
Biochemistry
July 12, 1988
Volume 27, Issue 14 5082-5088 doi: 10.1021/bi00414a020
Sekhar VC, Plapp BV.The binding of NAD+ to liver alcohol dehydrogenase was studied by stopped-flow techniques in the pH range from 6.1 to 10.9 at 25 degrees C. Varying the concentrations of NAD+ and a substrate analogue used to trap the enzyme-NAD+ complex gave saturation kinetics. The same maximum rate constants were obtained with or without the trapping agent and by following the reaction with protein fluorescence or absorbance of a ternary complex. The data fit a mechanism with diffusion-controlled association of enzyme and NAD+, followed by an isomerization with a forward rate constant of 500 s-1 at pH 8: E E... Investigation of intermediates and transition states in the catalytic mechanisms of active site substituted cobalt(II), nickel(II), zinc(II), and cadmium(II) horse liver alcohol dehydrogenase.
Biochemistry
January 19, 1982
Volume 21, Issue 2 354-363 doi: 10.1021/bi00531a024
Dunn MF, Dietrich H, MacGibbon AK, Koerber SC, Zeppezauer M.No abstract available Effects of urea and guanidine hydrochloride on the activity and dynamical structure of equine liver alcohol dehydrogenase.
Biochemistry
May 6, 1986
Volume 25, Issue 9 2471-2476 doi: 10.1021/bi00357a027
Strambini GB, Gonnelli M.The inactivation of equine liver alcohol dehydrogenase by guanidine hydrochloride and urea has been studied by monitoring the intrinsic tryptophan fluorescence and phosphorescence emission. The use of triplet-state lifetimes to probe the flexibility of protein structure at the site of tryptophan-314 reveals a distinct behavior between the two denaturants. At predenaturational concentrations, the loss of enzyme activity in guanidine hydrochloride is associated with a loosening of intramolecular interactions resulting in a greater fluidity of the interior region of the macromolecule. In contrast... A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide.
Biochemistry
February 11, 2004
Volume 43, Issue 6 1656-1666 doi: 10.1021/bi035531p
Cowley AB, Lukat-Rodgers GS, Rodgers KR, Benson DR.N-Acetylmicroperoxidase-8 (1) contains heme and residues 14-21 of horse mitochondrial cytochrome c (cyt c). The two thioether bonds linking protein to heme in cyt c are present in 1, and the native axial ligand His-18 remains coordinated to iron. As an approach to probing structural or functional roles played by the double covalent heme-protein linkage in cyt c, we have initiated a study in which the properties of 1 are compared with those of a synthetic mono-His coordinated heme peptide containing a single covalent linkage (2). One consequence of the greater conformational restriction imposed... Horse heart myoglobin catalyzes the H2O2-dependent oxidative dehalogenation of chlorophenols to DNA-binding radicals and quinones.
Biochemistry
August 4, 2007
Volume 46, Issue 34 9823-9829 doi: 10.1021/bi700684u
Osborne RL, Coggins MK, Walla M, Dawson JH.The heme-containing respiratory protein, myoglobin (Mb), best known for oxygen storage, can exhibit peroxidase-like activity under conditions of oxidative stress. Under such circumstances, the initially formed ferric state can react with H2O2 (or other peroxides) to generate a long-lived ferryl [Fe(IV)=O] Compound II (Cpd II) heme intermediate that is capable of oxidizing a variety of biomolecules. In this study, the ability of Mb Cpd II to catalyze the oxidation of carcinogenic halophenols is demonstrated. Specifically, 2,4,6-trichlorophenol (TCP) is converted to 2,6-dichloro-1,4-benzoquinone... FTIR analysis of the interaction of azide with horse heart myoglobin variants.
Biochemistry
June 21, 1994
Volume 33, Issue 24 7600-7608 doi: 10.1021/bi00190a013
Bogumil R, Hunter CL, Maurus R, Tang HL, Lee H, Lloyd E, Brayer GD, Smith M, Mauk AG.The interaction of azide with variants of horse heart myoglobin (Mb) has been characterized by Fourier transform infrared (FTIR), electron paramagnetic resonance (EPR), and UV-VIS absorption spectroscopy and by molecular modeling calculations. Distal histidine variants (His64Thr, His64Ile, His64Lys) and charged surface variants (Val67Arg, Lys45Glu, Lys45Glu/Lys63Glu) were included in this study. All variants, with the exception of Val67Arg, have a lower azide affinity than the wild-type protein. Analysis of the temperature dependence of the FTIR spectra (277-313 K) revealed that the wild-type ... Secretory proteins as potential semiochemical carriers in the horse.
Biochemistry
November 8, 2006
Volume 45, Issue 45 13418-13428 doi: 10.1021/bi061409p
D'Innocenzo B, Salzano AM, D'Ambrosio C, Gazzano A, Niccolini A, Sorce C, Dani FR, Scaloni A, Pelosi P.Two soluble proteins were isolated as major secretory products of horse sweat and of the parotid gland and characterized for structural and functional properties. The first protein, lipocalin allergen EquC1, was characterized for its glycosylation sites and bound glycosidic moieties. Only one (Asn53) of the two putative glycosylation sites within the sequence was post-translationally modified; a different glycosylation pattern was determined with respect to data previously reported. When purified from horse sweat, this protein contained oleamide and other organic molecules as natural ligands. ... Mutation of Asn-475 in the Venezuelan Equine Encephalitis Virus nsP2 Cysteine Protease Leads to a Self-Inhibited State.
Biochemistry
November 9, 2017
Volume 56, Issue 47 6221-6230 doi: 10.1021/acs.biochem.7b00746
Compton JR, Mickey MJ, Hu X, Marugan JJ, Legler PM.The alphaviral nsP2 cysteine protease of the Venezuelan equine encephalitis virus (VEEV) is a validated antiviral drug target. Clan CN proteases contain a cysteine protease domain that is intimately packed with an S-adenosyl-l-methionine-dependent RNA methyltransferase (SAM MTase) domain. Within a cleft formed at the interface of these two domains, the peptide substrate is thought to bind. The nucleophilic cysteine can be found within a conserved motif, NVCWAK, which differs from that of papain (CGSCWAFS). Mutation of the motif residue, N475, to alanine unexpectedly produced a self-inhibited s... Zinc isotope exchange in horse liver alcohol dehydrogenase.
Biochemistry
September 1, 1969
Volume 8, Issue 9 3792-3797 doi: 10.1021/bi00837a045
Drum DE, Li TK, Vallee BL.No abstract available The Specific Polysaccharide of Type XVIII Pneumococcus. III.
Biochemistry
November 1, 1963
Volume 2 1288-1294 doi: 10.1021/bi00906a020
ESTRADA-PARRA S, HEIDELBERGER M.No abstract available Identification of the lysine residue modified during the activation of acetimidylation of horse liver alcohol dehydrogenase.
Biochemistry
January 28, 1975
Volume 14, Issue 2 200-203 doi: 10.1021/bi00673a002
Dworschack R, Tarr G, Plapp BV.A single amino group in horse liver alcohol dehydrogenase was modified with methyl(14C)acetimidate by a differential labeling procedure. Lysine residues outside the active site were modified with ethyl acetimidate while a lysine residue in the active site was protected by the formation of an enzyme-NAD+-pyrazole complex. After the protecting reagents were removed, the enzyme was treated with methyl(14C)acetimidate. Enzyme activity was enhanced 13-fold as 1.1 (14C)acetimidyl group was incorporated per active site. A labeled peptide was isolated from a tryptic-chymotryptic digest of the modified... Two-dimensional 1H NMR studies of cytochrome c: assignment of the N-terminal helix.
Biochemistry
March 11, 1986
Volume 25, Issue 5 1100-1106 doi: 10.1021/bi00353a024
Wand AJ, Englander SW.The 1H resonances of 11 sequential amino acids in the N-terminal helix of horse ferrocytochrome c were studied by two-dimensional nuclear magnetic resonance techniques. All the main-chain protons from Lys-5 through Ala-15 and many of the side-chain protons were assigned. J-Correlated spectroscopy (COSY) was used to distinguish protons on neighboring bonds and to recognize amino acid types. Nuclear Overhauser effect spectroscopy (NOESY) was used to define spatially contiguous protons and to determine amino acid sequence neighbors. The relayed coherence experiment (relay COSY) was used to resolv... Structural features of the trans-activation response RNA element of equine infectious anemia virus.
Biochemistry
February 2, 1993
Volume 32, Issue 4 1096-1104 doi: 10.1021/bi00055a015
Hoffman DW, Colvin RA, Garcia-Blanco MA, White SW.A 25-nucleotide RNA with the sequence of the trans-activation response (TAR) element of equine infectious anemia virus (EIAV) was analyzed by biochemical methods and by one- and two-dimensional NMR spectroscopy. NMR, nuclease probing, and polyacrylamide gel migration rates show that the RNA consists of an A-helical stem capped by two non-Watson-Crick U-G base pairs and a compact four-nucleotide loop. The loop is stabilized by base stacking, with loop nucleotides C12 and C15 stacked upon U11 and G16, respectively. Near the 5' end of the molecule, the stem contains a bulge at nucleotide C2, most...
