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Your search keyword '"Min'kova NO"' showing total 4 results
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4 results on '"Min'kova NO"'

1. [Untitled]

Author

Lapteva Ti, Min'kova No, Filippovich IuB, E. V. Mikodina, and M. V. Samsonova

Subjects
chemistry.chemical_classification, Lipid composition, Fatty acid, Lipid metabolism, Liver lipid, medicine.anatomical_structure, Biochemistry, chemistry, Lipid content, Lens (anatomy), medicine, Normal lens, lipids (amino acids, peptides, and proteins), Alanine aminotransferase, Developmental Biology
Abstract

This papers opens a series of publications on the mechanisms of cataractogenesis in the salmon fry. Biochemical features of normal lens development and cataractogenesis in fry of different age and age-related dynamics of the liver lipid composition during upon cataractogenesis will be dealt with, since lipids are most intensely synthesized in the liver, from where they are transported in the lens. Here, we describe the dynamics of lens lipid composition in the salmon fry, including the total lipid content and dynamics of individual classes. The data are analyzed on the fatty acid spectrum of the salmon fry lens, as compared to the human lens.

Published
2003
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2. [Study of intracellular localization of the proteolytic enzyme complex and its protein inhibitors in bombyx grain].

Author

Iarygin DV, Min'kova NO, and Filippovich IuB

Subjects
Animals, Aspartic Acid Proteases metabolism, Cell Nucleus metabolism, Cysteine Proteases metabolism, Embryo, Nonmammalian cytology, Embryo, Nonmammalian metabolism, Hydrogen-Ion Concentration, Lysosomes metabolism, Mitochondria metabolism, Multienzyme Complexes metabolism, Serine Proteases metabolism, Subcellular Fractions, Bombyx embryology, Bombyx metabolism, Peptide Hydrolases metabolism, Protease Inhibitors metabolism
Abstract

Intracellular localization of serine, cysteine and aspartate proteases, as well as their protein inhibitors, in bombyx grain in the postdiapause period of embryogenesis has been studied. Proteolytic activity of aspartate and cysteine proteases was found in lysosomal, mitochondrial, and nuclear fractions of grains. Serine protease activity was not observed in subcellular fractions of grains of the fourth day of postdiapause development. It has been shown that activities of protein inhibitors and certain peptide hydrolases in subcellular fractions provide consistent functioning and fine regulation of the proteolytic enzyme complex.

Published
2012

3. [Aspartate- and alanine-aminotransferase in early development of keta].

Author

Samsonova MV, Min'kova NO, Lapteva TI, Mikodina EV, and Filippovich IuB

Subjects
Animals, Hydrogen-Ion Concentration, Alanine Transaminase metabolism, Aspartate Aminotransferases metabolism, Oncorhynchus growth & development
Abstract

We studied the activities of the marker enzymes of physiological state and adaptive reactions, aspartate and alanine aminotransferases, in early development of the keta Oncorhynchus keta. Aspartate aminotransferase with pH optima 6.8, 7.0, 7.6, and 8.0 and alanine aminotransferase with pH optima 7.0, 7.4, 7.6, 7.8, 8.0, and 8.2 were found in the eggs, larvae, and fry. The succession of enzymes with different pH takes place during ontogenesis, as well as stage specific changes in their activity. The maximum enzymatic activity was recorded in the larvae during their rise for "afloat." A correlation was established between the dynamics of enzymatic activity and soluble nitrogen and amine nitrogen contents.

Published
2003

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