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Monoclonal antibodies as molecular probes to study structural heterogeneity between human and animal renins and other aspartyl proteinases.

Publication ,  Journal Article
Dzau, VJ; Mudgett-Hunter, M; Haber, E
Published in: J Clin Endocrinol Metab
February 1986

Monoclonal antibodies may be helpful in comparing the structural homology of renins of various animal species as well as other aspartyl proteinases. We obtained four hybridoma lines secreting monoclonal antibodies that inhibited 3 Goldblatt mU human renin enzymatic activity with apparent IC50 of 1.1 X 10(-6)-4 X 10(-8) M. Each antibody was specific for human renin and did not cross-react either with other proteins tested nor with renins of other species in an immunoradiometric assay. These antibodies did not inhibit the enzymatic activities of nonprimate renins or nonrenin aspartyl proteinases tested. These data indicate that certain structural determinants of human renin activity may be uniquely different from those of nonprimate renins or nonrenin aspartyl proteinases.

Duke Scholars

Published In

J Clin Endocrinol Metab

DOI

ISSN

0021-972X

Publication Date

February 1986

Volume

62

Issue

2

Start / End Page

424 / 428

Location

United States

Related Subject Headings

  • Swine
  • Species Specificity
  • Renin
  • Rats
  • Mice
  • Humans
  • Endopeptidases
  • Endocrinology & Metabolism
  • Dogs
  • Chromatography, Affinity
 

Citation

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Dzau, V. J., Mudgett-Hunter, M., & Haber, E. (1986). Monoclonal antibodies as molecular probes to study structural heterogeneity between human and animal renins and other aspartyl proteinases. J Clin Endocrinol Metab, 62(2), 424–428. https://doi.org/10.1210/jcem-62-2-424
Dzau, V. J., M. Mudgett-Hunter, and E. Haber. “Monoclonal antibodies as molecular probes to study structural heterogeneity between human and animal renins and other aspartyl proteinases.J Clin Endocrinol Metab 62, no. 2 (February 1986): 424–28. https://doi.org/10.1210/jcem-62-2-424.
Dzau, V. J., et al. “Monoclonal antibodies as molecular probes to study structural heterogeneity between human and animal renins and other aspartyl proteinases.J Clin Endocrinol Metab, vol. 62, no. 2, Feb. 1986, pp. 424–28. Pubmed, doi:10.1210/jcem-62-2-424.
Journal cover image

Published In

J Clin Endocrinol Metab

DOI

ISSN

0021-972X

Publication Date

February 1986

Volume

62

Issue

2

Start / End Page

424 / 428

Location

United States

Related Subject Headings

  • Swine
  • Species Specificity
  • Renin
  • Rats
  • Mice
  • Humans
  • Endopeptidases
  • Endocrinology & Metabolism
  • Dogs
  • Chromatography, Affinity