Pepsinogen activation mechanism

Charles Sanny, J. A. Hartsuck, J. Tang

Research output: Contribution to journalArticle

Abstract

Activation of pepsinogen (Pg) to pepsin (P) by intramolecular cleavage has been deduced from previous work. Inherent proteolytic activity of Pg after conformational change in acid solutions has been suggested. These experimental data suggest that Pg is chemically converted to P by assaying the potential proteolytic activity of Pg which remains after various times of activation. Pg activated for 1.5 min at pH 2.85 shows no initial difference spectrum when pH is adjusted to 7.2, as reported by McPhie. However, subsequent incubation at pH 8.5 gradually produces a difference spectrum similar to that of Pg versus P indicating a dissociation of denatured P and the activation peptide. The first order activation rate constant calculated from the change in the difference spectra is 0.43/min which agrees with the constant previously reported. The chemical conversion of Pg to P under these conditions is also demonstrated by quantitative analysis of the N terminal 2 residues of the Pg and P in the activation mixture, after the proteins have been separated from the activation peptides.

Original languageEnglish
JournalFederation Proceedings
Volume33
Issue number5 II
StatePublished - 1 Jan 1974

Fingerprint

Pepsinogen A
Pepsin A
Peptides
Acids

Cite this

Sanny, C., Hartsuck, J. A., & Tang, J. (1974). Pepsinogen activation mechanism. Federation Proceedings, 33(5 II).
Sanny, Charles ; Hartsuck, J. A. ; Tang, J. / Pepsinogen activation mechanism. In: Federation Proceedings. 1974 ; Vol. 33, No. 5 II.
@article{fed8f3351a0a45648c784118cc7624c7,
title = "Pepsinogen activation mechanism",
abstract = "Activation of pepsinogen (Pg) to pepsin (P) by intramolecular cleavage has been deduced from previous work. Inherent proteolytic activity of Pg after conformational change in acid solutions has been suggested. These experimental data suggest that Pg is chemically converted to P by assaying the potential proteolytic activity of Pg which remains after various times of activation. Pg activated for 1.5 min at pH 2.85 shows no initial difference spectrum when pH is adjusted to 7.2, as reported by McPhie. However, subsequent incubation at pH 8.5 gradually produces a difference spectrum similar to that of Pg versus P indicating a dissociation of denatured P and the activation peptide. The first order activation rate constant calculated from the change in the difference spectra is 0.43/min which agrees with the constant previously reported. The chemical conversion of Pg to P under these conditions is also demonstrated by quantitative analysis of the N terminal 2 residues of the Pg and P in the activation mixture, after the proteins have been separated from the activation peptides.",
author = "Charles Sanny and Hartsuck, {J. A.} and J. Tang",
year = "1974",
month = "1",
day = "1",
language = "English",
volume = "33",
journal = "Federation Proceedings",
issn = "0014-9446",
number = "5 II",

}

Sanny, C, Hartsuck, JA & Tang, J 1974, 'Pepsinogen activation mechanism', Federation Proceedings, vol. 33, no. 5 II.

Pepsinogen activation mechanism. / Sanny, Charles; Hartsuck, J. A.; Tang, J.

In: Federation Proceedings, Vol. 33, No. 5 II, 01.01.1974.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Pepsinogen activation mechanism

AU - Sanny, Charles

AU - Hartsuck, J. A.

AU - Tang, J.

PY - 1974/1/1

Y1 - 1974/1/1

N2 - Activation of pepsinogen (Pg) to pepsin (P) by intramolecular cleavage has been deduced from previous work. Inherent proteolytic activity of Pg after conformational change in acid solutions has been suggested. These experimental data suggest that Pg is chemically converted to P by assaying the potential proteolytic activity of Pg which remains after various times of activation. Pg activated for 1.5 min at pH 2.85 shows no initial difference spectrum when pH is adjusted to 7.2, as reported by McPhie. However, subsequent incubation at pH 8.5 gradually produces a difference spectrum similar to that of Pg versus P indicating a dissociation of denatured P and the activation peptide. The first order activation rate constant calculated from the change in the difference spectra is 0.43/min which agrees with the constant previously reported. The chemical conversion of Pg to P under these conditions is also demonstrated by quantitative analysis of the N terminal 2 residues of the Pg and P in the activation mixture, after the proteins have been separated from the activation peptides.

AB - Activation of pepsinogen (Pg) to pepsin (P) by intramolecular cleavage has been deduced from previous work. Inherent proteolytic activity of Pg after conformational change in acid solutions has been suggested. These experimental data suggest that Pg is chemically converted to P by assaying the potential proteolytic activity of Pg which remains after various times of activation. Pg activated for 1.5 min at pH 2.85 shows no initial difference spectrum when pH is adjusted to 7.2, as reported by McPhie. However, subsequent incubation at pH 8.5 gradually produces a difference spectrum similar to that of Pg versus P indicating a dissociation of denatured P and the activation peptide. The first order activation rate constant calculated from the change in the difference spectra is 0.43/min which agrees with the constant previously reported. The chemical conversion of Pg to P under these conditions is also demonstrated by quantitative analysis of the N terminal 2 residues of the Pg and P in the activation mixture, after the proteins have been separated from the activation peptides.

UR - http://www.scopus.com/inward/record.url?scp=16744366918&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:16744366918

VL - 33

JO - Federation Proceedings

JF - Federation Proceedings

SN - 0014-9446

IS - 5 II

ER -

Sanny C, Hartsuck JA, Tang J. Pepsinogen activation mechanism. Federation Proceedings. 1974 Jan 1;33(5 II).