Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage.

Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage. Research Abstract Details 

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Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage. Abstract Text:

I A Khatri,G G Forstner,J F Forstner,

The present study reveals that partial proteolytic degradation of rat Muc 2 mucin can occur rapidly even in the presence of a battery of proteinase inhibitors. During the initial steps of purification from homogenates of intestinal scrapings, degradation was rapid, causing release of the entire 118 kDa C-terminal glycopeptide and, as shown by N-terminal sequencing, a large (200 kDa) N-terminal glycopeptide fragment. Degradation could be prevented by adding 6 M guanidinium chloride provided that its presence was maintained throughout every step of purification. Even after purification, however, the mucin was still vulnerable to partial proteolysis unless it was stored in guanidinium chloride at -20 degrees C. These findings imply that a potent proteinase contaminant remains tightly bound to the mucin through every step of purification, or else that the mucin has autocatalytic properties. Because the C- and N-terminal regions of secretory mucins are required for their assembly into linear mucin polymers that form functional gels, our findings emphasize that extreme care is required to purify structurally intact mucin molecules. They also imply that the specific degradation steps described here are likely to occur rapidly after mucins are secreted into the intestinal lumen and come into contact with the products of sloughed cells.

Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage. Publishing Authors By Initials

IA Khatri,GG Forstner,JF Forstner,

For similar animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: rats: rats, wistar research abstracts see: animals: chordata: vertebrates: mammals: rodentia: muridae: murinae: rats: rats, wistar research

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Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Biochemical journal

VOLUME: 331 ( Pt 1)

Page Numbers: 323-30

Journal Abbreviation: Biochem. J.

ISSN: 0264-6021

DAY: 1

MONTH: Apr

YEAR: 1998

Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage. Information

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LANGUAGE: eng

NlmUniqueID: 2984726

Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage. Keywords Mesh Terms:

KEYWORDS: Rats, Wistar

MESH TERMS: metabolism

Chemical & Substance for Abstract: Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage. Information

Substance Name: Peptide Fragments

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Grant and Affiliation Information for Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage.

AFFILIATION: Research Institute, The Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada.

Country: ENGLAND

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MEDLINETA: Biochem J

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