Evidence for the presence of an endogenous cytosolic protein inhibitor of intestinal fucosyltransferase activities.

Abstract:

:Soluble endogenous inhibitory activities for glycoprotein: alpha (1-2) and alpha (1-3) fucosyltransferases are demonstrated in rat small intestinal cytosol. These inhibitors are retained on DEAE-cellulose and are eluted as two fractions A and B. Fraction B is non dialyzable, heat stable and pronase-resistant and consists probably of poly-nucleotides. Fraction A is also non-dialyzable, but is thermolabile and pronase-sensitive, suggesting that it contains proteins. The inhibition of fucosyltransferase activity by fraction A is competitive for GDP-fucose and non-competitive for the glycoprotein substrate. Inhibition is not due to interfering enzymatic activities (glycosyl-nucleotide pyrophosphatases, glycosidases or proteases) and is reversible. This protein inhibitor, with a molecular weight of 60,000, is found only in the intestine and the pancreas and appears to be different from the previously reported inhibitors of brain glycolipid glycosyltransferases.

authors

Martin A,Ruggiero-Lopez D,Biol MC,Louisot P

doi

10.1016/0006-291x(90)90913-8

subject

Has Abstract

pub_date

1990-01-30 00:00:00

pages

1024-31

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)90913-8

journal_volume

166

pub_type

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