BIOCHEMICAL PROPERTIES OF CARBOXYPEPTIDASE A FROM NON-TRANSFERRED TISSUE AND BENIGNANT TUMOR TISSUE OF THE MAMMALIAN GLAND
Journal Title: Вісник Одеського національного університету. Біологія - Year 2016, Vol 21, Issue 2
Abstract
Introduction. Lysosomal carboxypeptidase A [КE 3.4.17.1] is a zinc-dependent protease that participates actively at the terminal stages of proteolysis and regulation of metabolism of cells in many physiological and pathological processes. Purpose. To study biochemical properties of carboxypeptidase A from non-transformed tissue and benignant tumor tissue of the mammalian gland. Methods. Sampling of anatomical materials for research was conducted with compliance of ethical and legal standards. Excretion of the enzymes included gradual fractionation with the (NH4)2SO4, dialysis in presence of 2.0 мМ Zn++ and gel chromatography on the sephadex – G 75. The investigation of the substrate specificity of the enzymes was held by hydrolysis of the substrate of carbobenzoxyphenylalanine, phenylalanylalanine, glutamyltyrosine, prolylalanine (2.0 mM), haemoglobin and casein (2.0 %). The influence of inhibitors and activators was determined in presence of: DTT, Zn++, cysteine, triton X-100, soybean trypsin inhibitor, leupeptin, pepstatin, PHMB, FMSF, dimethylmolyemydanhydride, tozylheptanol, mercaptoethanol, EDTA and 1.10 - phenanthroline. The maximal velocity (Vmax), Mihaelis constant (Km), inhibition type and inhibition constant (Ki) analysed by Laynuiveru – Berku method. Results. Carboxypeptidase A from non-transformed tissue and benignant tumor of the mammalian gland better splits the substrates, which have hydrophobic and aromatic amino acids. The activity of carboxypeptidase A from the benignant tumor of the mammalian gland is inhibited most of all under influence of leupeptin, tozylheptanol and dimethylmolyemydanhydride, in contrast to non-transformed tissue. For carboxypeptidase A from non-transformed tissue of the mammalian gland Km = 0.24 mM and Ki = 0.40 mM were determined, for carboxypeptidase A from the benignant tumor tissue of the mammalian gland – Km = 0.14 mM and Ki = 0.16 mM. Conclusion. Carboxypeptidase A from non-transformed tissue and benignant tumor of the mammalian gland is identical as to the substrate specificity, inhibition by phenylalanine for noncompetitive type, inhibition and activation effect by reagent with the exclusion of leupeptin, tozylheptanol and dimethylmolyemydanhydride, but differ as to affinity to carbobenzoxyphenylalanine and sensitivity to phenylalanine.
Authors and Affiliations
K. A. Filiptsova, I. L. Vovchuk
Keywords
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