Biokhimii︠a︡.
Publisher:
Obʺedinennoe nauchno-tekhnicheskoe izd-vo,. Moskva : Izdatelstvo Nauka
Frequency: Monthly, 1976-
Country: Russia (Federation)
Language: Russian
Author(s):
Institut biokhimii (Akademii︠a︡ nauk SSSR), Rossiĭskai︠a︡ akademii︠a︡ nauk.
Start Year:1936 -
Identifiers
| ISSN: | 0320-9725 (Print) 0320-9725 (Linking) |
| NLM ID: | 0372667 |
| (DNLM): | B16060000(s) |
| (OCoLC): | 01536412 |
| Coden: | BIOHAO |
| LCCN: | 50055899 |
| Classification: | W1 BI668 |
[Multiple forms of horse pepsin]. Using ion-exchange and affinity chromatography and isoelectrofocusing, eight forms of pepsin with pI 1.6, 1.8, 2.1, 2.3, 2.6, 2.8, 3.2 and 3.6, were isolated from horse gastric juice. The molecular weights, amino acid composition, N-terminal sequence and functional activity of these multiple forms were determined. Partial primary structure of tryptic peptides of pepsin with pI 2.3 was investigated. The analyzed partial sequences of the forms with pI 1.8, 2.1, 2.3, and 2.6 have identical structures which differ from the amino acid sequence of pepsin with pI 3.2 by four substituents. In terms of...
[Study of conformational changes in alcohol dehydrogenase during its interaction with silochrome adsorbent by the EPR spectroscopy method]. The possible use of EPR spectroscopy (spin labelling) for the study of horse liver alcohol dehydrogenase with a silochrome adsorbent is discussed. The rotatory diffusion of nitroxyl labels chemically linked to the enzyme was studied with reference to the time of the enzyme incubation with the adsorbent and the degree of its accumulation on the adsorbent surface. The mobility of nitroxyl radicals attached to the protein globules was shown to increase with time. It was concluded that the conformation of the enzyme molecules changes during their interaction with the adsorbent.
[Study of hydrolysis of aminoalcohol ethers, phenol and choline under the action of horse blood serum cholinesterase]. Hydrolysis of ethers of saturated and unsaturated alcohols and ethers, e.g. phenol and choline, under the action of horse blood serum cholinesterase, was studied. The reactivity towards enzymatic hydrolysis is decreased due to a greater length of the chain in the alcohol residue of the benzoic acid aminoethers; at nCH2 = 4 the compound is a poor substrate. An increase in nydrophobicity of the acyl residue of the ether molecule also leads to a decrease in the Vmax and Km values. In case of cholinesterase substrates, an increase in the molecule hydrophobicity results in an increase of its non-pr...
[Equine pepsins]. 6 forms of pepsin are found in horse gastric juice. Amino acid sequence is determined of N-terminal (most variable) part of polypeptide chain of main pepsin components. Equine pepsines, which have pI 2.1 and 2.3, are found to have identical amino acid sequence at least for 31 amino acid residues. The same sequence is observed in the component with pI 2.6 for 10 first residues. The sequence of equine pepsin with pI 3.2 has 3 substitutions for 33 amino acids, when compared with pepsines having pI 2.1 and 2.3. The forms of equine pepsin studied are more similar than the other isoenzyme pair, huma...