Chlamydomonas agglutinin is a hydroxyproline-rich glycoprotein
Author(s) -
James B. Cooper,
W. Steven Adair,
Robert P. Mecham,
John E. Heuser
Publication year - 1983
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.80.19.5898
Subject(s) - glycoprotein , agglutinin , lectin , soybean agglutinin , chlamydomonas , hydroxyproline , biochemistry , wheat germ agglutinin , phytohemagglutinins , concanavalin a , chemistry , biology , in vitro , gene , immunology , immune system , lymphocyte activation , t cell , mutant
Themt + sexual agglutinin fromChlamydomonas reinhardi is shown to contain ≈12% hydroxyproline, and two inhibitors of hydroxyproline formation, α,α′-dipyridyl and 3,4-dehydroproline, are shown to block the production of agglutinin activity in anin vivo bioassay system. These results indicate that the agglutinin glycoprotein may be related to a class of hydroxyproline-rich glycoproteins found in the extracellular matrix of higher plants, several of which have been shown to have lectin activity.
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