Conversion of pepsinogen to pepsin. Further evidence for intramolecular and pepsin catalyzed activation

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

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Exposure of pepsinogen to acid for less than 2 min yields a product with proteolytic activity. This activity is due to intramolecular and intermolecular formation of pepsin from pepsinogen. No evidence was found for intermolecular proteolytic activity in the zymogen. These conclusions are based upon 2 sets of experiments. First, chemical cleavage of pepsinogen during short activation is demonstrated by quantitative analysis of the NH2 terminal 2 residues of the pepsin and pepsinogen in an activation mixture. In addition, quantitative NH2 terminal analyses after activation under different condition confirm a previous inference that the product of unimolecular pepsinogen activation is homogeneous whereas bimolecular activation produces a pepsin product with a variety of NH2 termini. Second, spectral changes which occur upon acidification of a pepsinogen solution and are reversed by neutralization are shown to be consistent with the chemical cleavage of pepsinogen during acidification. The first order rate constant for pepsinogen activation, calculated from these spectral experiments, agrees well with the value determined previously.

Original languageEnglish
Pages (from-to)2635-2639
Number of pages5
JournalJournal of Biological Chemistry
Volume250
Issue number7
StatePublished - 1 Dec 1975

Fingerprint

Pepsinogen A
Pepsin A
Chemical activation
Acidification
Activation Analysis
Enzyme Precursors
Rate constants
Experiments
Acids

Cite this

@article{9082266f8ae14cb682b4c45871b41085,
title = "Conversion of pepsinogen to pepsin. Further evidence for intramolecular and pepsin catalyzed activation",
abstract = "Exposure of pepsinogen to acid for less than 2 min yields a product with proteolytic activity. This activity is due to intramolecular and intermolecular formation of pepsin from pepsinogen. No evidence was found for intermolecular proteolytic activity in the zymogen. These conclusions are based upon 2 sets of experiments. First, chemical cleavage of pepsinogen during short activation is demonstrated by quantitative analysis of the NH2 terminal 2 residues of the pepsin and pepsinogen in an activation mixture. In addition, quantitative NH2 terminal analyses after activation under different condition confirm a previous inference that the product of unimolecular pepsinogen activation is homogeneous whereas bimolecular activation produces a pepsin product with a variety of NH2 termini. Second, spectral changes which occur upon acidification of a pepsinogen solution and are reversed by neutralization are shown to be consistent with the chemical cleavage of pepsinogen during acidification. The first order rate constant for pepsinogen activation, calculated from these spectral experiments, agrees well with the value determined previously.",
author = "Charles Sanny and Hartsuck, {J. A.} and J. Tang",
year = "1975",
month = "12",
day = "1",
language = "English",
volume = "250",
pages = "2635--2639",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "7",

}

Conversion of pepsinogen to pepsin. Further evidence for intramolecular and pepsin catalyzed activation. / Sanny, Charles; Hartsuck, J. A.; Tang, J.

In: Journal of Biological Chemistry, Vol. 250, No. 7, 01.12.1975, p. 2635-2639.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Conversion of pepsinogen to pepsin. Further evidence for intramolecular and pepsin catalyzed activation

AU - Sanny, Charles

AU - Hartsuck, J. A.

AU - Tang, J.

PY - 1975/12/1

Y1 - 1975/12/1

N2 - Exposure of pepsinogen to acid for less than 2 min yields a product with proteolytic activity. This activity is due to intramolecular and intermolecular formation of pepsin from pepsinogen. No evidence was found for intermolecular proteolytic activity in the zymogen. These conclusions are based upon 2 sets of experiments. First, chemical cleavage of pepsinogen during short activation is demonstrated by quantitative analysis of the NH2 terminal 2 residues of the pepsin and pepsinogen in an activation mixture. In addition, quantitative NH2 terminal analyses after activation under different condition confirm a previous inference that the product of unimolecular pepsinogen activation is homogeneous whereas bimolecular activation produces a pepsin product with a variety of NH2 termini. Second, spectral changes which occur upon acidification of a pepsinogen solution and are reversed by neutralization are shown to be consistent with the chemical cleavage of pepsinogen during acidification. The first order rate constant for pepsinogen activation, calculated from these spectral experiments, agrees well with the value determined previously.

AB - Exposure of pepsinogen to acid for less than 2 min yields a product with proteolytic activity. This activity is due to intramolecular and intermolecular formation of pepsin from pepsinogen. No evidence was found for intermolecular proteolytic activity in the zymogen. These conclusions are based upon 2 sets of experiments. First, chemical cleavage of pepsinogen during short activation is demonstrated by quantitative analysis of the NH2 terminal 2 residues of the pepsin and pepsinogen in an activation mixture. In addition, quantitative NH2 terminal analyses after activation under different condition confirm a previous inference that the product of unimolecular pepsinogen activation is homogeneous whereas bimolecular activation produces a pepsin product with a variety of NH2 termini. Second, spectral changes which occur upon acidification of a pepsinogen solution and are reversed by neutralization are shown to be consistent with the chemical cleavage of pepsinogen during acidification. The first order rate constant for pepsinogen activation, calculated from these spectral experiments, agrees well with the value determined previously.

UR - http://www.scopus.com/inward/record.url?scp=0016705993&partnerID=8YFLogxK

M3 - Article

C2 - 235522

AN - SCOPUS:0016705993

VL - 250

SP - 2635

EP - 2639

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 7

ER -