The primary structure of high density apolipoprotein-glutamine-I.

Abstract:

:The major protein constituent of human plasma high density lipoproteins has been isolated and its complete amino-acid sequence determined. The protein, designated apolipoprotein-glutamine-I by the presence of carboxyl-terminal glutamine, is a single polypeptide chain of 245 amino-acid residues, including three residues of methionine. The protein is devoid of cysteine, cystine, and isoleucine. Cleavage of apolipoprotein-glutamine-I with cyanogen bromide yields four fragments with 94, 90, 36, and 25 amino acids. The amino-acid sequence of each fragment was determined by conventional methods, with proteolytic digestion with trypsin, chymotrypsin, and thermolysin. The alignment of the cyanogen bromide fragments was determined by the isolation of the methionine-containing tryptic peptides from apolipoprotein-glutamine-I. Inspection of the sequence of apolipoprotein-glutamine-I suggests an interesting distribution of amino acids that may account for its helical structure and its ability to bind and transport lipid.

authors

Baker HN,Delahunty T,Gotto AM Jr,Jackson RL

doi

10.1073/pnas.71.9.3631

subject

Has Abstract

pub_date

1974-09-01 00:00:00

pages

3631-4

issue

9

eissn

0027-8424

issn

1091-6490

journal_volume

71

pub_type

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