Abstract:
:Large glucagon immunoreactive substances, extracted from the fetal bovine pancreas and separated by gel filtration in the presence of 6 M guanidinium-hydrochloride, were submitted to lectin-sepharose affinity column chromatograph. Gel-filtered peak I (approximately 45 K delta) and peak II (approximately 10 K delta) interacted biospecifically with concanavalin-A- and wheat-germ-lectin-sepharoses, suggesting glycoproteins as possible constituents of large glucagon immunoreactive substances in extracts of the fetal bovine pancreas. The glucagon-like immunochemical identity of the lectin-sepharose-bound substances was further substantiated by binding to antiglucagon antibodies-sepharose and by characteristic proportional dilutions in the glucagon radioimmunoassay.
journal_name
Diabetesjournal_title
Diabetesauthors
Tung AK,Cockburn E,Siu KPdoi
10.2337/diacare.31.11.1002subject
Has Abstractpub_date
1982-11-01 00:00:00pages
1002-5issue
11eissn
0012-1797issn
1939-327Xjournal_volume
31pub_type
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