A NOVEL HEPARIN-BINDING PROTEIN, HBP15, IS IDENTIFIED AS MAMMALIAN RIBOSOMAL-PROTEIN L22

被引：14

作者：

FUJITA, Y

OKAMOTO, T

NOSHIRO, M

MCKEEHAN, WL

CRABB, JW

WHITNEY, RG

KATO, Y

SATO, JD

TAKADA, K

机构：

[1] HIROSHIMA UNIV,SCH DENT,DEPT BIOCHEM,MINAMI KU,HIROSHIMA 734,JAPAN

[2] W ALTON JONES CELL SCI CTR INC,LAKE PLACID,NY 12946

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 199卷 / 02期

关键词：

D O I：

10.1006/bbrc.1994.1286

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：

A 15kDa-protein (HBp15) was purified from mouse submandibular gland and bovine brain by virtue of its heparin-binding property. The amino acid sequences of mouse and bovine HBp15 showed a high degree of homology to a sea urchin protein encoded by gene called ''development specific protein 217.'' Using reverse transcription-polymerase chain reaction methods, cDNA clones for HBp15 were isolated from submandibular gland mRNA of mouse, human and pig, and sequenced. Database search of HBp15 showed that HBp15 also resembles yeast ribosomal protein YL31 in addition to the 217 protein. Using specific antibodies against HBp15, HBp15 was identified as mammalian ribosomal protein L22, for which no sequence information is available. (C) 1994 Academic Press, Inc.

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页码：706 / 713

页数：8

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