Cathepsins D from normal and some human neoplasms

Cathepsins D were isolated from human liver and spleen, from three malignant tumours (kidney cancer, sarcoma, spleen tumour caused by chronic myeloleucosis) and from one non-malignant tumour (uterine myoma). The isolation procedure involved adsorption on pepstatin-Sepharose and gel-filtration on Sep...

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Bibliographic Details
Published inBiokhimiia (Moscow, Russia) Vol. 44; no. 10; p. 1762
Main Authors Kazakova, O V, Orekhovich, V N
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.10.1979
Subjects
Cathepsins - metabolism
Female
Humans
Kidney Neoplasms - enzymology
Kinetics
Leiomyoma - enzymology
Liver - enzymology
Male
Molecular Weight
Neoplasms - enzymology
Organ Specificity
Sarcoma - enzymology
Spleen - enzymology
Splenic Neoplasms - enzymology
Substrate Specificity
Uterine Neoplasms - enzymology
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Summary:Cathepsins D were isolated from human liver and spleen, from three malignant tumours (kidney cancer, sarcoma, spleen tumour caused by chronic myeloleucosis) and from one non-malignant tumour (uterine myoma). The isolation procedure involved adsorption on pepstatin-Sepharose and gel-filtration on Sephadex G-100. A comparative study of the properties of these enzymes was carried out. The molecular weights, specific proteolytic activity toward hemoglobin and the synthetic hexapeptide Acetyl-Val-Val-Leu-Ser-Leu-Thr, carbohydrate content and type of dissociation of the molecules into polypeptide fragments during electrophoresis in the presence of DS-Na were determined. All the enzymes under study had molecular weights of about 45 000 except uterine myoma cathepsins (mol. weight 95 000). The latter cathepsin also differed from the other enzymes in its higher carbohydrate content.
ISSN:0320-9725