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Biochimica et biophysica acta.

Discontinued
Periodical
Biochemistry
Biophysics
Publisher:
Elsevier Pub. Co.
Frequency: One hundred issues per year, 2006-
Country: Netherlands
Language: English
Start Year:1947 - 2016
ISSN:
0006-3002 (Print)
1878-2434 (Electronic)
0006-3002 (Linking)
Impact Factor
6.2
2022
NLM ID:0217513
(OCoLC):01536398
(DNLM):B15340000(s)
Coden:BBACAQ
LCCN:49048142
Classification:W1 BI652
Purification and some molecular properties of horse liver acyl phosphatase.
Biochimica et biophysica acta    October 12, 1972   Volume 284, Issue 2 485-496 doi: 10.1016/0005-2744(72)90147-7
Ramponi G, Nassi P, Cappugi G, Treves C, Manao G.No abstract available
Effect of calcium ion on horse parathyroid gland adenyl cyclase.
Biochimica et biophysica acta    September 19, 1972   Volume 284, Issue 1 227-234 doi: 10.1016/0005-2744(72)90061-7
Matsuzaki S, Dumont JE.No abstract available
The autoxidation of horse hemoglobin: the effect of glutathione.
Biochimica et biophysica acta    June 26, 1972   Volume 273, Issue 1 30-39 doi: 10.1016/0304-4165(72)90188-2
Rifkind JM.The reduced glutathione in the erythrocyte was found to inhibit the autoxidation of purified horse hemoglobin. It was observed that much higher concentrations of oxidized glutathione also stabilize hemoglobin. The stabilization by oxidized glutathione most likely involves the formation of a mixed disulfide with the reactive β-93 sulfhydryl groups on the hemoglobin. A similar effect is also observed with N-ethyl- maleimide and HgCl2 which also react with the sulfhydryl groups. The apparent stabilization by reduced glutathione is partially due to the reduction of ferrihemoglobin formed by autox...
Imidazole: an inhibitor of L-phenylalanine-insensitive alkaline phosphatases of tissues other than intestine and placenta.
Biochimica et biophysica acta    May 12, 1972   Volume 268, Issue 2 415-421 doi: 10.1016/0005-2744(72)90337-3
Brunel C, Cathala G.1. Alkaline phosphatases (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) from brain, kidney, liver, bone, lung and spleen, which are not very sensitive to l-phenylalanine, are strongly inhibited by imidazole, whereas the placental and intestinal enzymes, which are very sensitive to l-phenylalanine, are only slightly affected. This is a new possibility for distinguishing the alkaline phosphatase isoenzymes. 2. The inhibition is apparently of an uncompetitive type, suggesting that the inhibitor interacts with the ES complex to form an EIS complex. 3. Histidine acts upon all enzyme...
Chemical and immunochemical studies on pregnant mare serum gonadotropin.
Biochimica et biophysica acta    March 15, 1972   Volume 263, Issue 1 139-148 doi: 10.1016/0005-2795(72)90168-7
Schams D, Papkoff H.Highly purified pregnant mare serum gonadotropin (PMSG) can be prepared from crude commercial preparations of PMSG by chromatography on sulfoethyl-Sephadex C-50 and gel filtration on Sephadex G-100. The preparation was examined by disc electrophoresis and gel filtration and found to be of high purity. Amino acid analysis shows similarities to pituitary gonadotropins. The PMSG contains a high content of proline and cystine and low amounts of the aromatic amino acids. Phenylalanine is the major amino terminal amino acid. The carbohydrate content totals 45% of which 10% is the content of sialic a...
Influence of chemical modifications of the reactive SH groups on the proton binding behaviour of human and horse hemoglobin.
Biochimica et biophysica acta    June 29, 1971   Volume 236, Issue 3 777-779 doi: 10.1016/0005-2795(71)90262-5
Janssen LH, de Bruin SH, van OS GA.No abstract available
On the electron-transfer-coupled proton release of cytochrome c.
Biochimica et biophysica acta    April 6, 1971   Volume 234, Issue 1 57-61 doi: 10.1016/0005-2728(71)90129-0
Czerlinski GH, Dar K.No abstract available
Water-soluble phosphates in horse granulocytes and lymphocytes.
Biochimica et biophysica acta    January 1, 1971   Volume 230, Issue 3 487-494 doi: 10.1016/0304-4165(71)90178-4
Meyer J, Bartlett GR.No abstract available
H-exchange behaviour and extent of reversible conformation changes in human, bovine, ovine, porcine and equine growth hormones.
Biochimica et biophysica acta    November 17, 1970   Volume 221, Issue 2 290-296 doi: 10.1016/0005-2795(70)90269-2
Cambiaso CL, Retegui LA, Dellacha JM, Santomé JA, Paladini AC.No abstract available
Preparation and properties of smooth muscle myosin from horse esophagus.
Biochimica et biophysica acta    September 1, 1970   Volume 216, Issue 2 411-421 doi: 10.1016/0005-2728(70)90233-1
Yamaguchi M, Miyazawa Y, Sekine T.Myosin was prepared from smooth muscle of horse esophagus in good yield (about 15 ° mg/Ioo g tissue) and was designated myosin S. Its properties were compared with those of myosin A from skeletal muscle. The ratio of the absorption of myosin S at 280 nm to that at 26o nm was about 1.8, and the amount of contaminating phosphorus was only o.91 g/io 5 g of myosin S, indicating that the latter is free of nucleic acid. The purity of this protein was examined by ultracentrifugation, gel filtration in the presence of 0.5 M KC1 and 6 M urea and chromatography on DEAE-cellulose columns. These e...
Microheterogeneity in ferritin molecules.
Biochimica et biophysica acta    April 28, 1970   Volume 207, Issue 1 256-258 doi: 10.1016/0005-2795(70)90158-3
Drysdale JW.No abstract available
N-Terminal sequences of equine and human immunoglobulin heavy chains.
Biochimica et biophysica acta    February 17, 1970   Volume 200, Issue 2 258-266 doi: 10.1016/0005-2795(70)90169-8
Montgomery PC, Bello AC, Rockey JH.N-terminal tetrapeptides from heavy chains of equine γGab- and γT-globulins, and of human γG and γA myeloma proteins and a γM macroglobulin, have been studied. The equine and human heavy chains lacked free α-amino-terminal groups. After mild alkaline hydrolysis, glutamic acid was identified as the terminal amino acid by reaction with dimethylaminonaphthalenesulfonyl chloride, tentatively identifying pyrrolid-2-one-5-carboxylic acid (PCA) as the unreactive terminal residue of each heavy chain. Peptides lacking a free α-amino group were isolated from subtilisin and pronase digests of the ...
Comparison of the resistance of human and horse ferrihemoglobin ligand derivatives to acid denaturation.
Biochimica et biophysica acta    December 23, 1969   Volume 194, Issue 2 364-375 doi: 10.1016/0005-2795(69)90097-x
Molday RS, Steinhardt J.No abstract available
Studies on the structure of ferritin and apoferritin from horse spleen. I. Tryptic digestion of ferritin and apoferritin.
Biochimica et biophysica acta    November 11, 1969   Volume 194, Issue 1 34-42 doi: 10.1016/0005-2795(69)90176-7
Crichton RR.No abstract available
Common and species-specific serum esterases of Equidae. I. Horse and donkey.
Biochimica et biophysica acta    January 1, 1969   Volume 191, Issue 3 611-620 doi: 10.1016/0005-2744(69)90354-4
Kaminski M.No abstract available
The sialic acids of horse serum with special reference to their virus inhibitory properties.
Biochimica et biophysica acta    March 11, 1968   Volume 156, Issue 2 317-326 doi: 10.1016/0304-4165(68)90261-4
Pepper DS.No abstract available
A comparative study of the multiplicity of mammalian esterases.
Biochimica et biophysica acta    January 8, 1968   Volume 151, Issue 1 147-158 doi: 10.1016/0005-2744(68)90169-1
Holmes RS, Masters CJ.Multiple forms of soluble esterase activity have been resolved in horse, sheep, ox and possum tissue extracts and sera. 2. By comparing esterase zymograms from different tissues and from different species, it is apparent that the distribution and multiplicity of esterase activity is tissue and species specific. 3. By means of substrate and inhibitor studies, the esterase multiple forms have been characterized into four main classes : carboxylesterases, arylesterases, acetylesterases, and cholinesterases. Each of these can be considered as an isoenzymic group. 4. Evidence is presented for furth...
Lipid composition of erythrocytes in various mammalian species.
Biochimica et biophysica acta    October 2, 1967   Volume 144, Issue 2 221-232 doi: 10.1016/0005-2760(67)90152-x
Nelson GJ.No abstract available
5hydroxytryptamine in interstitial cells of foetal equine gonads.
Biochimica et biophysica acta    August 24, 1965   Volume 107, Issue 1 158-160 doi: 10.1016/0304-4165(65)90409-5
Pace E.No abstract available
An improved method for preparation of follicle stimulating and luteinizing hormones from horse pituitary glands.
Biochimica et biophysica acta    July 8, 1965   Volume 104, Issue 2 496-502 doi: 10.1016/0304-4165(65)90355-7
Saxena BB, Henneman PH.No abstract available
Molecular Orientation in Horse Hemoglobin Crystals and Sickled Erythrocytes.
Biochimica et biophysica acta    January 25, 1965   Volume 94 194-199 doi: 10.1016/0926-6585(65)90024-5
MURAYAMA M, OLSON RA, JENNINGS WH.No abstract available
Characterization of Trichloroacetic Acid-Soluble Plasma Protein and Its Variations in Renal Insufficiency.
Biochimica et biophysica acta    July 7, 1964   Volume 83 231-236 doi: 10.1016/0926-6526(64)90040-0
STENZEL KH, LUBASH GD, DAVISON PF, RUBIN AL.No abstract available
The effect of thyroid hormones on oxygen consumption of isolated horse leucocytes.
Biochimica et biophysica acta    February 5, 1963   Volume 69 420-422 doi: 10.1016/0006-3002(63)91282-4
HAMOLSKY MW, MICHEL R, CARNICERO H, ROCHE J.No abstract available
Purification of follicle-stimulating hormone from horse anterior pituitary glands.
Biochimica et biophysica acta    December 17, 1962   Volume 65 394-402 doi: 10.1016/0006-3002(62)90439-0
SAXENA BB, McSHAN WH, MEYER RK.Fresh horse-pituitary glands were extracted with 40% ethanol and the gonadotropins were recovered by increasing the alcohol concentration to 85% followed by drying with acetone. This preparation was further extracted with water at pH 5, and the extract was adjusted to pH 7 and lyophilized. The follicle-stimulating hormone in the pH-5-souluble fraction was purified by zone electrophoresis and resolved into six components by starch-gel electrophoresis. One of these components contained follicle-stimulating hormone which was recovered in the elution cell and the contaminating starch was separated...
A note on the dielectric dispersion of deuterium oxide solutions of horse hemoglobin.
Biochimica et biophysica acta    June 1, 1959   Volume 33, Issue 2 576-578 doi: 10.1016/0006-3002(59)90158-1
TAKASHIMA S, LUMRY R.No abstract available
[New data on the structure of horse myoglobin].
Biochimica et biophysica acta    May 1, 1959   Volume 33, Issue 1 143-149 doi: 10.1016/0006-3002(59)90507-4
HOLLEMAN JW, BISERTE G.No abstract available
[Purification and structure of oxytocin and vasopressin from horses].
Biochimica et biophysica acta    February 1, 1959   Volume 31, Issue 2 545-548 doi: 10.1016/0006-3002(59)90033-2
ACHER R, CHAUVET J, LENCI MT.No abstract available
Residual glycogen at high ultimate pH in horse muscle.
Biochimica et biophysica acta    June 1, 1955   Volume 17, Issue 2 282-283 doi: 10.1016/0006-3002(55)90366-8
LAWRIE RA.No abstract available
The application of Edman’s peptide degradation method to horse myoglobin and haemoglobin.
Biochimica et biophysica acta    April 1, 1955   Volume 16, Issue 4 599-600 doi: 10.1016/0006-3002(55)90290-0
INGRAM VM.No abstract available
[Study of the amino acids formed by hydrolysis of horse globin by crystalline pepsin, trypsin and chymotrypsin].
Biochimica et biophysica acta    April 1, 1952   Volume 8, Issue 4 450-458 doi: 10.1016/0006-3002(52)90071-1
ROVERY M, DESNUELLE P.No abstract available