PARTIAL SEQUENCE OF THE PURIFIED PROTEIN CONFIRMS THE IDENTITY OF CDNA CODING FOR HUMAN LYSOSOMAL ALPHA-MANNOSIDASE-B

被引:19
作者
EMILIANI, C
MARTINO, S
STIRLING, JL
MARAS, B
ORLACCHIO, A
机构
[1] UNIV LONDON KINGS COLL, DIV LIFE SCI, LONDON W8 7AH, ENGLAND
[2] UNIV ROMA LA SAPIENZA, DIPARTIMENTO SCI BIOCHIM, ROME, ITALY
[3] UNIV ROMA LA SAPIENZA, CNR, CTR BIOL MOLEC, ROME, ITALY
关键词
D O I
10.1042/bj3050363
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
Human lysosomal alpha-mannosidase has been purified by a simple and rapid method in sufficient quantities for the analysis of its subunit composition and partial protein sequencing. Analysis of the N-terminal residues of the 30 kDa polypeptide has enabled a for us to confirm the identity of the recently cloned cDNA that was tentatively identified as that of lysosomal alpha-mannosidase [Nebes and Schmidt (1994) Biochem. Biophys. Res. Commun. 200, 239-245] and to locate the position of this polypeptide within the total deduced amino acid sequence. This finding will therefore provide a firm foundation for the characterization of alpha-mannosidosis mutations.
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页码:363 / 366
页数:4
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