Search Results

You are looking at 1 - 3 of 3 items for

  • Author: J. BORNSTEIN x
  • Refine by access: All content x
Clear All Modify Search
C. W. BAIRD
Search for other papers by C. W. BAIRD in
Google Scholar
PubMed
Close
and
J. BORNSTEIN
Search for other papers by J. BORNSTEIN in
Google Scholar
PubMed
Close

SUMMARY

An assay of insulin using adrenalectomized diabetic mice has been applied to the study of the insulin-like activity of plasma extracts.

It has been found that the insulin activity increases in normal subjects in response to the ingestion of carbohydrate, and that two groups of diabetics exist, those without and those with circulating insulin in plasma.

The significance of these findings in the aetiology of diabetes mellitus is discussed.

The limitations of the technique in the study of diabetes are emphasized.

Restricted access
J. BORNSTEIN
Search for other papers by J. BORNSTEIN in
Google Scholar
PubMed
Close
,
C. H. GRAY
Search for other papers by C. H. GRAY in
Google Scholar
PubMed
Close
, and
DELPHINE M. V. PARROTT
Search for other papers by DELPHINE M. V. PARROTT in
Google Scholar
PubMed
Close

An acid acetone extract of human plasma has been shown to be active in partially maintaining the weight and histological structure of the adrenals of hypophysectomized rats. As extracts of this type have been previously shown to be active in the Sayer's test, it appears that ACTH may be demonstrable in human plasma.

Restricted access
C. J. DRIVER
Search for other papers by C. J. DRIVER in
Google Scholar
PubMed
Close
,
J. McD. ARMSTRONG
Search for other papers by J. McD. ARMSTRONG in
Google Scholar
PubMed
Close
,
J. BORNSTEIN
Search for other papers by J. BORNSTEIN in
Google Scholar
PubMed
Close
, and
F. M. NG
Search for other papers by F. M. NG in
Google Scholar
PubMed
Close

SUMMARY

A peptidase has been isolated from ovine pituitary glands and has been purified. It specifically hydrolyses ovine growth hormone, releasing a peptide with somantin activity. It is proposed to call this peptidase somantin-releasing enzyme (SRE). It is a di-isopropylphosphorofluoridate-sensitive peptidase with a molecular weight of 23000 Daltons. It is optimally active near pH 8·0. It is of quite limited specificity, as it hydrolysed growth hormone to a limited extent only and did not hydrolyse most of the other proteins tested as substrates.

Restricted access