Literature DB >> 3510128

Comparative studies on lens neutral endopeptidase and pituitary neutral proteinase: two closely similar enzymes.

K Ray, H Harris.   

Abstract

A neutral endopeptidase (EC 3.4.24.5) previously thought to be unique to the eye lens has been found to be closely similar if not identical in native molecular size, component polypeptides and antigenic structure to a neutral proteinase from pituitary. Here we investigated some subtle differences in properties of the two enzymes, such as the effects of temperature, divalent cations and SDS on their activities with respect to different substrates. We conclude that the pituitary enzyme may have a relatively more compact structure requiring relaxation by low SDS concentration or higher temperature for maximum activity.

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Year:  1986        PMID: 3510128     DOI: 10.1016/0014-5793(86)80057-6

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Properties of subunits of the multicatalytic proteinase complex revealed by the use of subunit-specific antibodies.

Authors:  A J Rivett; S T Sweeney
Journal:  Biochem J       Date:  1991-08-15       Impact factor: 3.857

2.  Lens neutral endopeptidase occurs in other bovine and human tissues.

Authors:  K Ray; H Harris
Journal:  Biochem J       Date:  1987-12-15       Impact factor: 3.857

  2 in total

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