Robert Cherniak cherrc at PANTHER.GSU.EDU
Mon Dec 18 17:46:52 EST 1995

I have a low Mol. Wt. glycopeptide (~20kD) isolated from a yeast that is 
heavily glycosylated, mainly with mannose.  The majority of the linkages 
are reducing termini and 1->2 linked.  There are low levels of other 
linkages and other sugars. The major amino acids are serine(20) and 
threonine(17); alanine(13); aspartic acid (11) and glutamic acid (11); 
glycine (4), valine (4), leucine (5), and proline (6).  No histidine, 
lysine, others >1.  Amino acids released from the deglycosylated pepitide 
are serine, aspartic acid, threonine, alanine, and valine.  At the third 
cycle the amino acids are the same and in a constant ratio.  Aspartic acid 
and serine are released from the glycosylated peptide only during the first 
sequencing cycle.  No release occurs on additional sequence cycles.  The 
peptide is responsible for cell mediated immunity to the yeast.
Is this a common structural motif for a O-glycosylated peptide?
Any other comments are welcome.

Dr. Robert Cherniak                 Voice: (404)651-3868
Dept. of Chemistry                    Fax: (404)651-1416
Georgia State University           E-mail: cherniak at gsu.edu
Atlanta, GA 30303

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