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Mass Spectrometric Characterization of the β-Subunit of Human Chorionic Gonadotropin

✍ Scribed by Liu, ChuanLiang; Bowers, Larry D.

Publisher
John Wiley and Sons
Year
1997
Tongue
English
Weight
458 KB
Volume
32
Category
Article
ISSN
1076-5174

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✦ Synopsis

A high-performance liquid chromatographic/electrospray mass spectrometric (HPLC/MS) technique is described for the characterization of the b-subunit of the glycopeptide human chorionic gonadotropin (hCG). The b-subunit of hCG was dissociated from the a-subunit using 0.1% triÑuoroacetic acid (TFA) and separated by reversed-phase HPLC using a 0.1% TFA-acetonitrile gradient. Although reductive alkylation with 4-vinylpyridine allowed direct observation of the intact b-subunit of hCG by HPLC/MS due to the increase in charge, the heterogeneity of the carbohydrate fractions resulted in poor detection limits and extremely complex spectra. After reductive alkylation with either iodoacetate or 4-vinylpyridine, tryptic fragments of either the aor b-subunit can be observed using reversed-phase HPLC/MS. HPLC/MS data were consistent with the reported primary sequence, although oligosaccharide attachment sites at both 127Ser and 132Ser could not be documented. Microheterogeneity of the carbohydrate moiety on both N-glycosylation sites on the b-subunit could be readily observed. A larger degree of heterogeneity was observed on 13Asn. Di †erences were also observed in the oligosaccharide distribution in three commerial preparations of hCG. Detection of the C-terminal portion of the b-subunit required enzymatic deglycosylation prior to HPLC/MS analysis.

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