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Isolation and expression of a full-length cDNA encoding the human GM2 activator protein.

Abstract：

:We report the construction of a cDNA clone encoding a functional GM2-activator protein. The sequence of the complete 5' end of the coding region was determined by direct nucleotide sequencing of a fragment generated by multiple RACE PCR procedures from Hela cell cDNA. Specific oligonucleotides were synthesized from these data which allowed us to produce a PCR fragment that contained the complete coding sequence of the protein. This was then cloned into a mammalian expression vector. The ability of purified hexosaminidase A (beta-N-acetylhexosaminidase, EC 3.2.1.52) to hydrolyse labeled GM2 ganglioside was enhanced 10-fold more by the addition in the assay mix of lysate from transfected COS-1 cells than by the addition of identical amounts of lysate from mock transfected cells. Direct sequencing of PCR fragments from two sources also identified three polymorphisms.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Xie B,McInnes B,Neote K,Lamhonwah AM,Mahuran D

doi

10.1016/0006-291x(91)90671-s

subject

Has Abstract

pub_date

1991-06-28 00:00:00

pages

1217-23

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)90671-S

journal_volume

177

pub_type

杂志文章

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