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The Journal of Immunology, 1961, 87: 472-476.
Copyright © 1961 by The American Association of Immunologists, Inc.
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Antigenicity, Solubility and Chemical Stability of Renin Complexes1

Erwin Haas and Harry Goldblatt

From the Louis D. Beaumont Memorial Research Laboratories, Mount Sinai Hospital and the Department of Pathology, School of Medicine, Western Reserve University, Cleveland, Ohio

Abstract

The ability of renin to function as an antigen for the formation of antirenin and the inhibition of the pressor activity of renin by the immune serum have been reconfirmed. This capacity of renin to stimulate the formation of antienzymatic antibodies can be impaired greatly by coupling of the renin to certain polymers of high molecular weight such as sodium desoxyribonucleate, hyaluronic acid or chondroitin sulfate.

The pressor activity of the renin was unimpaired when it was in the form of the complexes. This indicates that the enzymatically active groupings (centers) in the renin molecule were not affected by the complex formation.

Renin was investigated further in combination with five additional compounds known to form complexes with proteins, but all of these failed to interfere with the activity of renin both as a pressor agent and as an antigen in the formation of antirenin.

The solubility of renin was enhanced considerably by complex formation with hyaluronic acid, chondroitin sulfate and protamine.

Renin exposed to n-heptane was completely inactivated, but it was protected and retained its pressor activity in the form of its complexes with oleic acid or lecithin.

Footnotes

This investigation was supported by grants from the National Heart Institute (H-1767), and the L. D. Beaumont Memorial Foundation, Cleveland, Ohio.






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