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Receptor binding and Nb2 cell mitogenic activities of glycosylated vs. unglycosylated porcine prolactin.

Abstract：

:Purified fractions of glycosylated (pGPrl) and unglycosylated (pUGPrl) porcine prolactin were prepared by affinity chromatography on Concanavalin A-Sepharose. The relative binding activities of these two forms of prolactin for receptors from porcine mammary, adrenal cortex and rabbit mammary, as well as their Nb2 cell mitogenic activity were determined. In both the porcine mammary and adrenal cortex receptor binding assays pGPrl had a 2-3 fold lower activity than pUGPrl. In the rabbit mammary binding assay pGPrl had a about a 5 fold lower activity than pUGPrl. Similarly, pGPrl had only about 20% of the activity of pUGPrl in the Nb2 cell proliferation assay.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Atkinson PR,Seely JE,Klemcke HG,Hughes JP

doi

10.1016/s0006-291x(88)81265-8

subject

Has Abstract

pub_date

1988-09-30 00:00:00

pages

1187-93

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)81265-8

journal_volume

155

pub_type

杂志文章

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