Skip to main content
Log in

Endogenous inhibitor of calcium activated neutral proteinase from human placenta: Purification and possible mechanism of proteinase regulation

  • Published:
Journal of Biosciences Aims and scope Submit manuscript

Abstract

An endogenous inhibitor of calcium activated neutral proteinase has been purified from human placenta. The procedure included chromatography on DEAE cellulose, Ultrogel AcA 22 and milli calcium activated neutral proteinase-sepharose in succession. Endogenous calcium activated neutral proteinase inhibitor was a tetramer with identical subunits of molecular weight 68 kDa. It was specific for milli calcium activated neutral proteinase (Calpain II) which is inhibited by the formation of an inactive enzyme-inhibitor complex and not by sequestering Ca2+ from the medium. Although micro calcium activated neutral proteinase (Calpain I) was not inhibited by endogenous calcium activated neutral proteinase inhibitor, it was protected from autolysis in the presence of the inhibitor. The placental endogenous calcium activated neutral proteinase inhibitor thus regulates Ca2+ activated proteolysis by ensuring micro calcium activated neutral proteinase activity, while inhibiting milli calcium activated neutral proteinase.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

CANP:

Calcium activated neutral proteinase

ECI:

endogenous CANP inhibitor

SDS:

sodium dodecyl sulphate

PAGE:

Polyacrylamide gel electrophoresis

PBS:

phosphate buffer saline

M r :

molecular weight

References

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Shastri, R., Shailaja, B. & Anandaraj, M.P.J.S. Endogenous inhibitor of calcium activated neutral proteinase from human placenta: Purification and possible mechanism of proteinase regulation. J Biosci 15, 435–442 (1990). https://doi.org/10.1007/BF02702685

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02702685

Keywords

Navigation