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Glycosylated human growth hormone (hGH): a novel 24 kDa hGH-N variant.

Abstract：

:We have identified a human pituitary protein as a novel glycosylated variant of hGH. Isolation of the denatured protein included separation of human pituitary extract by Sephadex G-100 chromatography in ammonium bicarbonate, followed by Sephadex G-100 chromatography in 10% acetic acid, with subsequent DEAE Sephacryl chromatography in ammonium bicarbonate, and finally by preparative SDS PAGE. The pituitary protein has a molecular weight of 24 kDa as determined by SDS PAGE analysis and is thus larger than the normal 22 kDa hGH. N-Terminal amino acid sequence analysis of the first twenty-six residues reveals that this protein is not derived from the hGH-V gene but is rather a hGH-N gene product. Assays for the detection of glycoconjugates (periodate oxidation, sialidase treatment, trifluoromethanesulfonic acid treatment) indicate that the hGH variant has carbohydrate moieties. The discovery of new hGH raises questions about the role of glycosylation in the structure/function relationships of this hormone.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Haro LS,Lewis UJ,Garcia M,Bustamante J,Martinez AO,Ling NC

doi

10.1006/bbrc.1996.1697

subject

Has Abstract

pub_date

1996-11-12 00:00:00

pages

549-56

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)91697-6

journal_volume

228

pub_type

杂志文章

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