| Literature DB >> 6546784 |
D J Chin, G Gil, D W Russell, L Liscum, K L Luskey, S K Basu, H Okayama, P Berg, J L Goldstein, M S Brown.
Abstract
The nucleotide sequence of a 4.8-kilobase mRNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase, the endoplasmic reticulum enzyme that controls cholesterol biosynthesis, shows that it is a protein of 887 amino acids (molecular weight 97,092) which contains three potential sites for asparagine-linked glycosylation. The reductase is a transmembrane glycoprotein, but in contrast to many other transmembrane glycoproteins, it lacks a cleavable or hydrophobic NH2-terminal signal sequence.Entities:
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Year: 1984 PMID: 6546784 DOI: 10.1038/308613a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962