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Normal human plasma alpha 2HS-glycoprotein has earlier been shown to be comprised of two polypeptide chains. Recently, the amino acid and carbohydrate sequences of the short chain were elucidated (Gejyo, F., Chang, J.-L., Bürgi, W., Schmid, K., Offner, G. D., Troxler, R.F., van Halbeck, H., Dorland, L., Gerwig, G. J., and Vliegenthart, J.F.G. (1983) J. Biol. Chem. 258, 4966-4971). In the present study, the amino acid sequence of the long chain of this protein, designated A-chain, was determined and found to consist of 282 amino acid residues. Twenty-four amino acid doublets were found; the most abundant of these are Pro-Pro and Ala-Ala which each occur five times. Of particular interest is the presence of three Gly-X-Pro and one Gly-Pro-X sequences that are characteristic of the repeating sequences of collagens. Chou-Fasman evaluation of the secondary structure suggested that the A-chain contains 29% alpha-helix, 24% beta-pleated sheet, and 26% reverse turns and, thus, approximately 80% of the polypeptide chain may display ordered structure. Four glycosylation sites were identified. The two N-glycosidic oligosaccharides were found in the center region (residues 138 and 158), whereas the two O-glycosidic heterosaccharides, both linked to threonine (residues 238 and 252), occur within the carboxyl-terminal region. The N-glycans are linked to Asn residues in beta-turns, while the O-glycans are located in short random segments. Comparison of the sequence of the amino- and carboxyl-terminal 30 residues with protein sequences in a data bank demonstrated that the A-chain is not significantly related to any known proteins. However, the proline-rich carboxyl-terminal region of the A-chain displays some sequence similarity to collagens and the collagen-like domains of complement subcomponent C1q.
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
April 1983,
The Journal of biological chemistry,
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
June 1984,
Proceedings of the National Academy of Sciences of the United States of America,
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
February 1988,
Proceedings of the National Academy of Sciences of the United States of America,
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
July 1998,
Carbohydrate research,
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
November 1979,
Biochemistry,
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
August 1980,
Proceedings of the National Academy of Sciences of the United States of America,
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
March 1990,
The Journal of biological chemistry,
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
February 1981,
Biochemical and biophysical research communications,
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
November 1981,
Biochimica et biophysica acta,
Y Yoshioka, and
F Gejyo, and
T Marti, and
E E Rickli, and
W Bürgi, and
G D Offner, and
R F Troxler, and
K Schmid
April 1986,
Proceedings of the National Academy of Sciences of the United States of America,
