ISOFORMS OF TURKEY PROLACTIN - EVIDENCE FOR DIFFERENCES IN GLYCOSYLATION AND IN TRYPTIC PEPTIDE-MAPPING

被引：25

作者：

CORCORAN, DH ^{[1
]}

PROUDMAN, JA ^{[1
]}

机构：

[1] USDA ARS,BELTSVILLE AGR RES CTR,AVIAN PHYSIOL LAB,BELTSVILLE,MD 20705

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1991年 / 99卷 / 03期

关键词：

D O I：

10.1016/0305-0491(91)90338-E

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：

1. Three isoforms of turkey pituitary proclactin have been isolated, including a nonglycosylated isoform of 22,500 mol. wt and two glycosylated isoforms of 24,500 mol. wt. 2. The glycosylated turkey prolactins differed in carbohydrate composition, with one isoform apparently containing only O-linked carbohydrate. 3. Tryptic peptide maps showed a few peptides distinctly different among the three prolactin isoforms. 4. Amino acid sequencing of the first 40 residues of the three prolactin isoforms showed arginine at position 24 and histidine at position 27, for the nonglycosylated form, but no identifiable amino acids were detected at this position for the glycosylated isoforms.

引用

页码：563 / 570

页数：8

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