JOE
HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Journal of Endocrinology (1982) 93, 169-176    DOI: 10.1677/joe.0.0930169
© 1982 Society for Endocrinology

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chowdhury, M.
Right arrow Articles by Steinberger, E.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Chowdhury, M.
Right arrow Articles by Steinberger, E.

Further characterization of the molecular species formed during the biosynthesis of rat luteinizing hormone

M. Chowdhury, H. E. Grotjan, Jr and E. Steinberger

During the biosynthesis of rat LH (rLH) there are four molecular species found intracellularly: native rLH, a species which co-elutes with rLH{alpha} on Sephadex G-100, a species which elutes with an apparent molecular weight of approximately 21 000 and a large molecular weight form (excluded from Sephadex G-100). Significant quantities of native rLH and rLH{alpha} are secreted. The species of large molecular weight binds to Concanavalin A–Sepharose suggesting that it is glycosylated. The 21 000 molecular weight rLH-like molecule has tentatively been identified as an rLH subunit which has not been completely processed.







HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1982 by the Society for Endocrinology.