ISSN:
1573-4986
Keywords:
cinnamomin
;
glycopeptides
;
NMR
;
primary structure
;
ribosome-inactivating protein
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Cinnamomin is a plant type II ribosome-inactivating protein (RIP) isolated from the seeds of Cinnamomum camphora. It consists of two nonidentical polypeptide chains (A- and B-chain) held together through one disulfide linkage. Its A- and B-chain contain 0.3% and 3.9% sugars respectively. The B-chain of cinnamomin was digested by pronase E and then the liberated glycopeptides were separated from non-glycopeptides by gel filtration chromatography on a Bio-Gel P-4 column. Three crude glycopeptides were obtained by continuing chromatography over anion-exchange resin (AG1-X2) in the buffer of 2% pyridine-acetic acid (pH 8.3) with a polygradient elution system. Through further purification by the gel filtration chromatography and HPLC, three major glycopeptides, GP1, GP2 and GP3 were obtained. Mainly by two-dimensional Nuclear Magnetic Resonance (NMR) including TOCSY, DQF-COSY, NOESY, HMQC and HMBC, their primary structures were analyzed as: Manα1,3Manα1,6(Manα1,3)(Xylβ1,2)Manβ1,4GlcNAcβ1,4GlcNAcβ1-(Gly-)Asn-Asn-Thr(GP1), Manα1,6(Manα1,3)(Xylβ1,2)Manβ1,4GlcNAcβ1,4(Fucα1,3)GlcNAcβ1-Asn-Ala-Thr(GP2),Manα1,6(Manα1,3)Manα1,6(Manα1,2 Manα1,3)Manβ1,4GlcNAcβ1,4GlcNAcβ1-(Ala-)Asn-Gly-Thr(GP3).
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1010957007038
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