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[Primary structure of the cytoplasmic aspartate aminotransferases from the swine myocardium. Isolation, purification and characteristics of the peptides from cyanogen bromide cleavage].

Cytoplasmic aspartate aminotransferase from pig heart muscle was cleaved with cyanogen bromide and 8 peptide fragments were isolated. The high tendency of the large peptides for aggregation was overcome only by the utilization of special procedures of the denaturation and acylation of the lysine residues of peptide with citraconic anhydride. Peptides were separated by gel chromatography on sephadex G-50 and G-75 and by ion exchange chromatography on cellulose DE-22 and DE-32 with use of concentrated urea solutions. Amino acid composition and N-terminal residues of isolated peptides were determined.

Amino Acid Sequence↗
PubMed1976

[Modification of the number and structure of certain cytoplasmic components of the renal tubules during compensatory hypertrophy].

In the remaining kidney of unilaterally nephrectomised three to six months old Wistar rats, the measurement of the external and internal diameters indicated an increase in size of both proximal and distal convoluted tubules, although less distinct in the latter. Stereomorphometric measurements of the chondriome and the cytoplasmic inclusions (lysosomes, phagosomes, peroxisomes, etc.) have shown, as compared with similar tests in shamoperated animals, changes in the volumes of these components which can be related to the increase of enzymatic activities reported earlier. However, no obvious changes of the general ultrastructure of the kidneys undergoing hypertrophy could be observed.

Animals↗
PubMed1977

[Quaternary structure of a cytoplasmic protein with ribonuclease activity from wheate seedling leaves. Kinetic manifestation of its "native", dissociated and reassociated forms].

Previous data on oligomeric nature and values of molecular masses of "native" and dissociated forms of cytoplasmic protein with ribonulcease activity from wheat seedling leaves (Bezenchukskaya 98) are confirmed by means of polyacrylamide gel disc electrophoresis. Possible relation of the "native" enzyme form with 3':5'-cAMP is demonstrated by paper chromatography and the enzyme reassociation by the nucleotide. Study of kinetic manifestation of "native", dissociated and reassociated enzyme forms has revealed that the enzyme in the "normal" state has probably at least two active sites, "negative" homotropic cooperative interaction being establish-d between them at the definite degree of substrate saturation. The cooperativity disappears under dissociation, and it is discovered again under reassociation.

Binding Sites↗