Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1974 Feb;137(2):223–228. doi: 10.1042/bj1370223

Human placental cathepsin B1. Isolation and some physical properties

Arnold A Swanson 1, Bill J Martin 1, Sam S Spicer 1
PMCID: PMC1166108  PMID: 4824207

Abstract

A reproducible procedure for the isolation, from human placenta, of a cathepsin B1 in a homogeneous state, demonstrated by electrophoretic, ultracentrifugal and enzymic criteria, was carried out. The pH optimum was near pH5.5. The placental enzyme catalysed the release of acid-soluble u.v.-dense products from haemoglobin and myoglobin. It was inhibited by heavy metals and several compounds which react with the thiol groups. The optimum temperature was between 37° and 42°C. The molecular weight of the enzyme was calculated to be 24250.

Full text

PDF
224

Images in this article

226-1PLATE 1
on p.226-1
228Fig. 5.
on p.228

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BOUMA J. M., GRUBER M. THE DISTRIBUTION OF CATHEPSINS B AND C IN RAT TISSUES. Biochim Biophys Acta. 1964 Sep 18;89:545–547. doi: 10.1016/0926-6569(64)90082-3. [DOI] [PubMed] [Google Scholar]
  2. Barrett A. J. Human cathepsin B1. Purification and some properties of the enzyme. Biochem J. 1973 Apr;131(4):809–822. doi: 10.1042/bj1310809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Christie G. A. Comparative histochemical distribution of acid phosphatase, non-specific esterase and beta-glucuronidase in the placenta and foetal membranes. Histochemie. 1968;12(3):189–207. doi: 10.1007/BF00305996. [DOI] [PubMed] [Google Scholar]
  4. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  5. DURELL J., FRUTON J. S. Proteinase-catalyzed transamidation and its efficiency. J Biol Chem. 1954 Apr;207(2):487–500. [PubMed] [Google Scholar]
  6. FUJII S., FRUTON J. S. Transamidation reactions catalyzed by cathepsins. J Biol Chem. 1958 Jan;230(1):1–11. [PubMed] [Google Scholar]
  7. Fox H., Kharkongor F. N. Morphology and enzyme histochemistry of cells derived from placental villi in tissue culture. J Pathol. 1970 Jul;101(3):267–276. doi: 10.1002/path.1711010310. [DOI] [PubMed] [Google Scholar]
  8. Fox H., Kharkongor N. F. Enzyme histochemistry of the Hofbauer cells of the human placenta. J Obstet Gynaecol Br Commonw. 1969 Oct;76(10):918–921. doi: 10.1111/j.1471-0528.1969.tb15730.x. [DOI] [PubMed] [Google Scholar]
  9. GREENBAUM L. M., FRUTON J. S. Purification and properties of beef spleen cathepsin B. J Biol Chem. 1957 May;226(1):173–180. [PubMed] [Google Scholar]
  10. Gniot-Szulzycka J., Komoszyński M. Human placenta sulphohydrolase C subfractions. Enzymologia. 1972 Jan 31;42(1):11–21. [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. ORNSTEIN L. DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY. Ann N Y Acad Sci. 1964 Dec 28;121:321–349. doi: 10.1111/j.1749-6632.1964.tb14207.x. [DOI] [PubMed] [Google Scholar]
  13. Otto K. Uber ein neues Kathepsin. Reinigung aus Rindermilz, Eigenschaften, sowie Vergleich mit Kathepsin B. Hoppe Seylers Z Physiol Chem. 1967 Nov;348(11):1449–1460. [PubMed] [Google Scholar]
  14. TALLAN H. H., JONES M. E., FRUTON J. S. On the proteolytic enzymes of animal tissues. X. Beef spleen cathepsin C. J Biol Chem. 1952 Feb;194(2):793–805. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES