[Immunochemical study of bovine spleen thiol proteinases: cathepsinS B, H and L]. 1983

L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva

Rabbit antisera were prepared against three highly purified enzymes from bovine spleen: proteinase I (cathepsin L), proteinase II (cathepsin H), and cathepsin B. The Ouchterlony double diffusion test shows that each antiserum specifically reacts with the corresponding antigen and does not cross react with other proteinases. These data provide evidence that the three proteinases are distinct with respect to their antigenic properties. Using specific antisera, the identity of two preparations of proteinase I isolated by different methods was demonstrated. Analysis of the fractions obtained in the course of isolation procedure revealed a component reacting with antisera against proteinase I. It had a greater molecular mass than proteinase I (30 000-40 000), was richer in antigenic respect and had a lower proteolytic activity as compared with proteinase I. The effect of various inhibitors and denaturation conditions on antigenic properties of proteinases was also studied.

UI MeSH Term Description Entries
D010450 Endopeptidases A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. Endopeptidase,Peptide Peptidohydrolases
D002401 Cathepsin B A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS. Cathepsin B-Like Proteinase,Cathepsin B1,Cathepsin B Like Proteinase,Proteinase, Cathepsin B-Like
D002403 Cathepsins A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES. Cathepsin
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D003546 Cysteine Endopeptidases ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
D005779 Immunodiffusion Technique involving the diffusion of antigen or antibody through a semisolid medium, usually agar or agarose gel, with the result being a precipitin reaction. Gel Diffusion Tests,Diffusion Test, Gel,Diffusion Tests, Gel,Gel Diffusion Test,Immunodiffusions,Test, Gel Diffusion,Tests, Gel Diffusion
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000941 Antigens Substances that are recognized by the immune system and induce an immune reaction. Antigen
D013154 Spleen An encapsulated lymphatic organ through which venous blood filters.
D056655 Cathepsin H An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.

Related Publications

L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
January 1981, Acta biologica et medica Germanica,
L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
July 1984, Japanese journal of pharmacology,
L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
December 1984, Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire,
L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
July 1991, FEBS letters,
L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
December 1989, The Biochemical journal,
L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
February 1992, European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies,
L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
March 1985, FEBS letters,
L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
January 1991, Biomedica biochimica acta,
L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
January 1982, The Biochemical journal,
L A Lokshina, and I A Tarkhanova, and O N Lubkova, and N V Golubeva, and T A Gureeva
July 1999, Cancer biochemistry biophysics,
Copied contents to your clipboard!