Properties of human neutral bronchial mucins after modification of the peptide or the carbohydrate moieties.

Abstract:

:Trypsin and pronase treatment of purified human neutral bronchial mucins released small fragments from the C-terminal end of these molecules and resulted in slight increases in their sedimentation coefficient presumably reflecting conformational changes. The antigenic determinant of neutral bronchial mucins which appears to be located on this C-terminal fragment is destroyed by pronase or by treatments such as periodate oxidation or galactose oxidase-bromine oxidation which modify the carbohydrate moieties. Thus, both amino acid and carbohydrate residues are involved in the structure of the antigenic determinant.

journal_name

Biochimie

journal_title

Biochimie

authors

Lhermitte M,Lambin G,Lafitte JJ,Rousseau J,Degand P,Roussel P

doi

10.1016/s0300-9084(76)80444-0

subject

Has Abstract

pub_date

1976-01-01 00:00:00

pages

367-72

issue

3

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(76)80444-0

journal_volume

58

pub_type

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