GLYCOSYLATED HUMAN PROLACTIN - DETECTION BY IMMUNOBLOTTING OF BIOLOGICAL-FLUIDS IS CONFOUNDED BY ANTISERA CROSS-REACTIVITY WITH IMMUNOGLOBULINS

被引：7

作者：

HEFFNER, LJ ^{[1
]}

MARKOFF, E ^{[1
]}

YUAN, RW ^{[1
]}

LEE, DW ^{[1
]}

机构：

[1] CHILDRENS HOSP RES FDN, DIV ENDOCRINOL, CINCINNATI, OH 45229 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 212卷 / 01期

关键词：

D O I：

10.1006/bbrc.1995.1934

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Glycosylated human prolactin is found in several biological fluids and can only be detected by western immunoblotting. Glycosylated prolactin migrates at 25,000-27,000 molecular weight while prolactin migrates at 23,000. We have discovered that several antihuman prolactin sera crossreact with some light chain components of human immunoglobulins, which also migrate at 25,000 on electrophoretic gels run under reducing conditions. Evidence is provided for prolactin binding to immunoglobulins in biological fluids, which may explain why some polyclonal anti-prolactin sera demonstrate this crossreactivity. (C) 1995 Academic Press, Inc.

引用

页码：48 / 55

页数：8

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