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THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBIN

THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBIN Princeton, New Jersey) (Acceptedfor publication,June 9, 1938) In the hemoglobin method for the estimation of proteinase, denatured hemoglobin is digested under standard conditions, the undigested hemoglobin is precipitated with trichloracetic acid, and the amount of unprecipitated protein split products, which is a measure of the amount of proteinase present, is estimated with the phenol reagent which gives a blue color with tyrosine and tryptophane. Hemoglobin, unlike casein and gelatin, is a reproducible substrate. Different batches of hemoglobin are digested at the same rate by a given proteinasesolution. Even when peptidase is present in addition to proteinase, the formation of products not precipitable by trichloracetic acid is due so far as is known to proteinase alone. Hemoglobin methods have been described for pepsin (Anson and Mirsky, 1932), trypsin (Anson and Mirsky, 1933), papain (Anson, 1937a), and cathepsin (Anson, 1937 b). Since the methods were first worked out several minor errors have been corrected, the preparation of the hemoglobin substrates has been simplified, and the estimation procedures have been standardized. Rather than point out the numerous changes which have been made I have considered it simpler and more useful to describe completely the procedures as they are now used in http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of General Physiology Rockefeller University Press

THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBIN

M. L. Anson
The Journal of General Physiology , Volume 22 (1): 79 – Sep 1, 1938
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Publisher
Rockefeller University Press
Copyright
Copyright © 1938 by The Rockefeller University Press
ISSN
0022-1295
eISSN
1540-7748
DOI
10.1085/jgp.22.1.79
Publisher site
See Article on Publisher Site

Abstract

Princeton, New Jersey) (Acceptedfor publication,June 9, 1938) In the hemoglobin method for the estimation of proteinase, denatured hemoglobin is digested under standard conditions, the undigested hemoglobin is precipitated with trichloracetic acid, and the amount of unprecipitated protein split products, which is a measure of the amount of proteinase present, is estimated with the phenol reagent which gives a blue color with tyrosine and tryptophane. Hemoglobin, unlike casein and gelatin, is a reproducible substrate. Different batches of hemoglobin are digested at the same rate by a given proteinasesolution. Even when peptidase is present in addition to proteinase, the formation of products not precipitable by trichloracetic acid is due so far as is known to proteinase alone. Hemoglobin methods have been described for pepsin (Anson and Mirsky, 1932), trypsin (Anson and Mirsky, 1933), papain (Anson, 1937a), and cathepsin (Anson, 1937 b). Since the methods were first worked out several minor errors have been corrected, the preparation of the hemoglobin substrates has been simplified, and the estimation procedures have been standardized. Rather than point out the numerous changes which have been made I have considered it simpler and more useful to describe completely the procedures as they are now used in

Journal

The Journal of General Physiology – Rockefeller University Press

Published: Sep 1, 1938

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