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PubMedDate not supplied

[Characteristics of cysteine peptidohydrolases from the human kidney cortex].

Spectrum of cysteine peptide hydrolases was studied in human kidney cortex using a variety of protein and synthetic substrates after the preparation was fractionated on Sephadex G-100 following the precipitation with ammonium sulfate 40-70%. Activities of dipeptidyl aminopeptidase I, lysosomal carboxypeptidases A and B, cathepsins B and H, as well as the activity of Ca+2-dependent neutral proteinase were detected. A thiol-dependent proteolytic activity, which was apparently stimulated by cathepsin T- and -M like enzymes, was also observed. Besides, the proteinase with molecular mass of 50-60 KDa and high hemoglobin and casein splitting activity was found. This activity cannot be attributed to any of the proteinases so far known. Isoelectrofocusing technique showed that two forms of cathepsin B occurred in human kidney with isoelectric points at pH 5.32 and pH 5.65; two forms of cathepsin H were also detected exhibiting isoelectric points at pH 6.03 and pH 6.7.

Chromatography, Gel↗
PubMedDate not supplied

[A method of isolation of partially purified alkaline peptide hydrolase from Drosophila melanogaster larvae].

A semipreparative method is developed for preparing peptidohydrolase from Drosophila melanogaster larvae which involves the stages of extraction, salting-out, gel-filtration and ion-exchange chromatography. It is established that the maximal (up to 81%) yield of the enzyme is observed with the single extraction in the alkaline medium. The main bulk of the enzyme is salted-out in the low acid 3 M ammonium sulphate solution. Gel-filtration on column with Sephadex-25 provides complete salting-out of the enzyme-containing fraction, and ion exchange chromatography on CM-cellulose--a considerable purification of the enzyme under study. A degree of the obtained purification of the enzyme under study. A degree of the obtained peptidohydrolase preparation purity in acid and alkaline medium is determined by the method of electrophoresis in PAAG. At all stages of the preparation the enzyme possesses the casein-lytic activity and is able of hydrolyzing the ethyl ester and benzoyl arginine p-nitroanilide.

Animals↗
PubMedDate not supplied

[Peptide hydrolase activity in brain tissues during the early stages of post-hypothermia period].

The acid peptidohydrolase activity in the homogenate, dissoluble and mitochondrial-lysosomal fractions of brain tissues of rats who have endured deep hypothermia was determined after their "active" warming for an hour and on the 1st, 2nd, 3d and 7th days after their self-warming. The "active" warming of rats who have endured deep hypothermia (19-20 degrees C) brings about the restoration of the acid peptidohydrolase activity in the subcellular brain tissue fractions. After self-warming the examined enzyme activity restores 7 days later. In the dynamics of the posthypothermic period a change in the acid peptide hydrolase distribution in fractions occurs on the 2nd-3d days.

Animals↗
PubMedDate not supplied

[Activity of arginase and proteolytic processes in the brain and liver of rats in cold acclimatization].

The activity of arginase, neutral peptidohydrolase (protaminase) and total intensity of autolysis were determined in the brain and liver of rats on the 1st, 3d, 30th and 45th days animal stay at a temperature of 2-4 degrees C. in the process of rats acclimatization to cold there occurs a correlation in the brain - between the activity of arginase and neutral peptidohydrolase, in the liver - between the arginase activity and total proteolytical activity (autolysis).

Acclimatization↗
PubMedDate not supplied

[Ontogenic properties of peptidohydrolase activity in tissue extracts from Drosophila melanogaster].

The paper deals with the activity of peptidohydrolases splitting hemoglobin, casein and benzoylarginine-p-nitroanilide (BAPNA) in the ontogenesis of Drosophila mutant white apricot (wa). The enzymic activity is high in the intestine tissue at the larval stage, but it does not manifest itself at the pupal stage that may be due to inactivation of the studied enzymes by inhibitors found in extracts of the pupal tissues. The imaginal period of development is characterized by a low level of the peptidohydrolase activity in females and its absence in males in whose tissues there is a high content of inhibitors. The peptidohydrolase activity in extracts of larval tissues is established to be dependent completely on the enzyme being in the intestinal wall. Incomplete purification of this peptidohydrolase and its inhibitor is performed by means of ion-exchange chromatography on DEAE-cellulose. Some of their physicochemical properties are investigated.

Aging↗
PubMed1978

Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy.

Vicilin peptidohydrolase, the protease that hydrolyzes the reserve proteins in the cotyledons of mung bean (Vigna radiata) seedlings, has been localized intracellularly by immunofluorescence microscopy using monospecific antibodies against the enzyme and rhodamine-coupled goat-anti-rabbit immunoglobulin G's. The enzyme can first be visualized after 3 days of seedling growth and is associated with small foci within the cytoplasm of the storage parenchyma cells farthest from the vascular bundles. On the 4th day of growth, the protease is also present in the numerous large protein bodies within these cells. Vicilin peptidohydrolase is known to be synthesized de novo starting on the 3rd day of growth. Our observations are therefore consistent with the interpretation that the enzyme is synthesized in the cytoplasm and subsequently transported to the protein bodies.

Cytoplasm↗