Archives of biochemistry and biophysics.

Glycan profiling of a defect in decorin glycosylation in equine systemic proteoglycan accumulation, a potential model of progeroid form of Ehlers-Danlos syndrome.

Archives of biochemistry and biophysics June 17, 2010 Volume 501, Issue 2 221-231 doi: 10.1016/j.abb.2010.06.017

Kim B, Yoon JH, Zhang J, Eric Mueller PO, Halper J.Defects in glycosylation of decorin can result in systemic hereditary disease. A mutation in the galactosyl transferase I gene is the underlying defect of a progeroid form of Ehlers-Danlos syndrome. We have previously described pathological changes in equine systemic proteoglycan accumulation (ESPA, formerly degenerative suspensory ligament desmitis) as consisting of excessive presence of decorin and other proteoglycans in organs and structures with a high content of connective tissue. Using liquid chromatography/mass spectrometry, and one- and two-dimensional immunoblotting we have determined...

Archives of biochemistry and biophysics March 9, 2005 Volume 436, Issue 1 168-177 doi: 10.1016/j.abb.2005.01.016

Regis WC, Fattori J, Santoro MM, Jamin M, Ramos CH.The work in the literature on apomyoglobin is almost equally divided between horse and sperm whale myoglobins. The two proteins share high homology, show similar folding behavior, and it is often assumed that all folding phenomena found with one protein will also be found with the other. We report data at equilibrium showing that horse myoglobin was 2.1 kcal/mol less stable than sperm whale myoglobin at pH 5.0, and aggregated at high concentrations as measured by gel filtration and analytical ultracentrifugation experiments. The higher stability of sperm whale myoglobin was identified for both...

Archives of biochemistry and biophysics October 6, 2006 Volume 456, Issue 1 71-78 doi: 10.1016/j.abb.2006.09.014

Arkill KP, Winlove CP.Articular cartilage extracellular matrix imposes a significant transport barrier to albumin, the principal carrier of fatty acids. It has not been previously established whether it also influences the transport of fatty acids important for chondrocyte metabolism. Albumin was labelled with rhodamine-maleimide and bound to NBD-labelled lauric acid. Plugs of fresh equine metacarpal-phalangeal cartilage and subchondral bone were incubated with the complex at 4 degrees C for 2-160 h. The fluorophore distribution was quantified using quantitative microscopy in histological sections. The fluorescence...

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Horse Spleen Hemosiderin. I. Isolation.

Archives of biochemistry and biophysics March 1, 1964 Volume 104 487-495 doi: 10.1016/0003-9861(64)90493-x

MCKAY RH, FINEBERG RA.No abstract available

Archives of biochemistry and biophysics February 29, 2008 Volume 474, Issue 1 1-7 doi: 10.1016/j.abb.2008.02.032

Iniesta J, Cooper HJ, Marshall AG, Heptinstall J, Walton DJ, Peterson IR.The iodination of proteins remains a useful tool in biochemistry for radiolabelling. However, chemical or enzymatic iodination is difficult to control and can give deleterious polyiodination. Previously, we have shown that electrooxidation with nitrite is a rapid method for the selective nitration of tyrosine residues in proteins. In principle, it should be possible to substitute a number of electrooxidisable anions into the tyrosine phenol ring. Electrochemical iodination is more difficult to control than nitration because the rapid anodic oxidation of I(-) leads to persistent formation of th...

Archives of biochemistry and biophysics April 15, 1981 Volume 208, Issue 1 37-41 doi: 10.1016/0003-9861(81)90120-x

Stefani M, Liguri G, Berti A, Nassi P, Ramponi G.No abstract available

Archives of biochemistry and biophysics February 15, 1994 Volume 309, Issue 1 178-183 doi: 10.1006/abbi.1994.1100

Webb B, Frame J, Zhao Z, Lee ML, Watt GD.A procedure for trapping small molecules inside the interior of horse spleen ferritin (HoSF) and methods for characterizing HoSF and its small entrapped molecules are described. HoSF is first dissociated into subunits by adjustment to pH 2 in the presence of the small molecules to be trapped. The pH of the dissociated HoSF is then increased to 7 at which time the dissociated subunits reassemble reforming the 24-mer HoSF, thereby trapping solvent within its interior. HoSF is then separated from unbound molecules by dialysis, ultrafiltration, and/or ammonium sulfate precipitation. Sephadex G-25 ...

Archives of biochemistry and biophysics November 15, 1988 Volume 267, Issue 1 271-279 doi: 10.1016/0003-9861(88)90032-x

Torres JL, Rush RS, Main AR.The serine carboxylesterase from horse serum was characterized by amino acid composition, peptide mapping, molecular and subunit weights, and sequencing of the amino acids around the essential serine residue at the active site. A protocol was developed for using reversed-phase high-performance liquid chromatography as the final step to obtain homogeneous preparations of horse serum carboxylesterase. Amounts sufficient for determining the amino acid composition and for peptide maps were obtained from a partially purified starting material which contained approximately 55% carboxylesterase. The ...

Archives of biochemistry and biophysics December 1, 1960 Volume 91 319-325 doi: 10.1016/0003-9861(60)90507-5

AKESON A, THEORELL H.No abstract available

Archives of biochemistry and biophysics September 1, 1970 Volume 140, Issue 1 52-59 doi: 10.1016/0003-9861(70)90009-3

Mani JC, Pietruszko R, Theorell H.No abstract available

Archives of biochemistry and biophysics January 29, 2007 Volume 461, Issue 1 13-23 doi: 10.1016/j.abb.2007.01.007

Gorgoglione V, Laraspata D, La Piana G, Marzulli D, Lofrumento NE.The data reported are fully consistent with the well-known observation that exogenous cytochrome c (cyto-c) molecules do not permeate through the outer membrane of mitochondria (MOM) incubated in isotonic medium (250 mM sucrose). Cyto-c is unable to accept electrons from the sulfite/cyto-c oxido-reductase (Sox) present in the intermembrane space, unless mitochondria are solubilized. Mitochondria incubated in a very high hypotonic medium (25 mM sucrose), in contrast to any expectation, continue to be not permeable to added cyto-c even if Sox and adenylate kinase are released into the medium. Th...

Archives of biochemistry and biophysics November 9, 2000 Volume 382, Issue 2 284-295 doi: 10.1006/abbi.2000.2039

Taylor KC, Vitello LB, Erman JE.The ionization of 4-nitroimidazole to 4-nitroimidazolate was investigated as a function of ionic strength. The apparent pKa varies from 8.99 to 9.50 between 0.001 and 1.0 M ionic strength, respectively, at 25 degrees C. The ionic strength dependence of this ionization is anomalous. The binding of 4-nitroimidazole by horse metmyoglobin was studied between pH 5.0 and 11.5 and as a function of ionic strength between 0.01 and 1.0 M. The association rate constant is pH-dependent, varying from 24 M(-1)s(-1) at pH 5 to a maximum value of 280 M(-1)s(-1) at pH 9.5 and then decreasing to 10 M(-1)s(-1) a...

Archives of biochemistry and biophysics July 1, 1971 Volume 145, Issue 1 55-63 doi: 10.1016/0003-9861(71)90009-9

Lee JC, Harpst JA.No abstract available

Archives of biochemistry and biophysics November 1, 1976 Volume 177, Issue 1 284-292 doi: 10.1016/0003-9861(76)90438-0

Rose AB, Dube S.No abstract available

Archives of biochemistry and biophysics August 26, 2017 Volume 633 40-49 doi: 10.1016/j.abb.2017.08.015

Khan SH, Islam A, Hassan MI, Sharma S, Singh TP, Ahmad F.A sequence alignment of horse cytochrome c (cyt c) with all known cyts c shows that Leu at position 94 is conserved, except in 14 species which have either Val or Ile at this position. It is also known that Leu94 of the mammalian cyt c plays an important role in folding and stability. The important question here is as to what will happen in terms of folding and stability if Leu94 of the mammalian cyt c is substituted by Val or Ile. To answer this question, we introduced natural substitutes of Leu94 by Val and Ile in horse cyt c. The purified L94V and L94I mutants under native condition (pH 6.0...

Archives of biochemistry and biophysics February 24, 2009 Volume 485, Issue 1 49-55 doi: 10.1016/j.abb.2009.02.009

DiMaio Knych HK, DeStefano Shields C, Buckpitt AR, Stanley SD.Substantial gaps exist in our knowledge of the metabolic clearance of therapeutic agents in horses. Accordingly, a cytochrome P450 monooxygenase in the 2C family was cloned from an equine liver, sequenced and expressed in a baculovirus expression system. Catalytic activities of the recombinant protein were measured with a number of substrates. The protein, assigned CYP2C92, displayed optimal catalytic activity with diclofenac using molar ratios of CYP2C92 to NADPH CYP450 reductase of 1:18. Addition of cytochrome b(5) to diclofenac incubations had no significant effect on metabolic turnover. CY...

Archives of biochemistry and biophysics October 15, 1983 Volume 226, Issue 2 414-424 doi: 10.1016/0003-9861(83)90310-7

Manao G, Camici G, Stefani M, Berti A, Cappugi G, Liguri G, Nassi P, Ramponi G.Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enz...

Archives of biochemistry and biophysics January 26, 1999 Volume 362, Issue 1 148-158 doi: 10.1006/abbi.1998.0991

Lin J, Merryweather J, Vitello LB, Erman JE.The kinetics of formation and dissociation of the horse metmyoglobin/azide complex has been investigated between pH 3.5 and 11.5. The ionic strength dependence of the reaction has been determined at integral pH values between 5 and 10. Hydrazoic acid, HN3, binds to metmyoglobin with a rate constant of (3.8 +/- 1.0) x 10(5) M-1 s-1. Protonation of a group with an apparent pKa of 4.0 +/- 0.3 increases the rate of HN3 binding 6.5-fold to (2.5 +/- 0.8) x 10(6) M-1 s-1. The ionizable group is attributed to the distal histidine, His-64. The azide anion, N-3, binds to metmyoglobin with a rate constan...

Archives of biochemistry and biophysics March 1, 1969 Volume 130, Issue 1 362-369 doi: 10.1016/0003-9861(69)90045-9

Ramponi G, Guerritore A, Treves C, Nassi P, Baccari V.No abstract available

Archives of biochemistry and biophysics September 1, 1976 Volume 176, Issue 1 71-81 doi: 10.1016/0003-9861(76)90142-9

Teng TL, Harpst JA, Lee JC, Zinn A, Carlson DM.No abstract available

Archives of biochemistry and biophysics July 1, 1972 Volume 151, Issue 1 353-355 doi: 10.1016/0003-9861(72)90507-3

Jauregui-Adell J, Cladel G, Ferraz-Pina C, Rech J.No abstract available

Archives of biochemistry and biophysics November 1, 1987 Volume 258, Issue 2 621-629 doi: 10.1016/0003-9861(87)90385-7

Vitello LB, Erman JE.The binding of horse heart cytochrome c to yeast cytochrome c peroxidase in which the heme group was replaced by protoporphyrin IX was determined by a fluorescence quenching technique. The association between ferricytochrome c and cytochrome c peroxidase was investigated at pH 6.0 in cacodylate/KNO3 buffers. Ionic strength was varied between 3.5 mM and 1.0 M. No binding occurs at 1.0 M ionic strength although there was a substantial decrease in fluorescence intensity due to the inner filter effect. After correcting for the inner filter effect, significant quenching of porphyrin cytochrome c pe...

Archives of biochemistry and biophysics December 1, 1991 Volume 291, Issue 2 291-299 doi: 10.1016/0003-9861(91)90137-8

Rae C, Board PG, Kuchel PW.In mammalian red blood cells the metabolism of methylglyoxal, and some alpha-ketoaldehydes, takes place via two, generally, highly active enzymes, glyoxalase 1 and 2. The 1H NMR spin-echo spectra of horse erythrocytes, and the various reactants in the glyoxalase system, were characterized as a prelude to obtaining series of spectra in time courses of methylglyoxal metabolism. We characterized the kinetics of the enzyme system in red cells from a normal horse and also from one which had very low activity of glyoxylase 2. The kinetics of the reaction scheme, with methylglyoxal as the starting su...

Archives of biochemistry and biophysics March 1, 1967 Volume 119, Issue 1 552-559 doi: 10.1016/0003-9861(67)90490-0

Oppenheimer HL, Green RW, McKay RH.No abstract available

Archives of biochemistry and biophysics January 1, 1964 Volume 104 27-31 doi: 10.1016/s0003-9861(64)80030-8

COLACICCO G.No abstract available

Archives of biochemistry and biophysics January 1, 1983 Volume 220, Issue 1 208-213 doi: 10.1016/0003-9861(83)90402-2

Li CH, Chung D.Isolation of prolactin from equine pituitary glands has been described. It has a potency of 42 IU/mg in the pigeon crop-sac test and consists of 199 amino acids. The hormone has only four half-cystine residues in contrast to other mammalian prolactins which have six residues. From NH2-terminal sequence analysis and amino acid composition of cyanogen bromide fragments, the NH2-terminal disulfide loop is missing in the equine prolactin molecule. Circular dichroism spectra indicate that the alpha-helical content of equine prolactin appears to be lower (50%) than that found in the ovine hormone (6...

Archives of biochemistry and biophysics June 1, 1968 Volume 125, Issue 3 975-980 doi: 10.1016/0003-9861(68)90536-5

Mainwaring WI, Hofmann T.No abstract available

Archives of biochemistry and biophysics April 1, 1971 Volume 143, Issue 2 354-358 doi: 10.1016/0003-9861(71)90221-9

Theorell H, Tatemoto K.No abstract available

Archives of biochemistry and biophysics May 1, 1963 Volume 101 225-228 doi: 10.1016/s0003-9861(63)80006-5

SUZUKI K, MIYOSAWA Y, SUZUKI C.No abstract available

Archives of biochemistry and biophysics July 20, 2000 Volume 380, Issue 1 165-173 doi: 10.1006/abbi.2000.1912

Tkachenko AG, Winston GW.Preincubation of horse liver alcohol dehydrogenase (HLADH) with the oxidative agent, tert-butyl hydroperoxide (tBOOH) results in a twofold stimulation of the ethanol dehydrogenase activity of this enzyme. This stimulation was dependent on tBOOH concentration up to 100 mM; above this concentration tBOOH did not further stimulate ethanol oxidation by HLADH. Active-site-directed reagents and classical ADH binary complexes were used to probe the possible mechanism of this activating effect. The rate and extent of stimulation by tBOOH is strongly reduced by binary complexes with NAD(+) or NADH, who...

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NLM ID:	0372430
(DNLM):	A60645000(s)
(OCoLC):	01482120
Coden:	ABBIA4
LCCN:	44005905
Classification:	W1 AR449

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