Saul Jarcho's contribution to the history of paleopathology.
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Historiography↗
Biomedical subjects
E Cockburn
Publications and source records attributed to E Cockburn.
Beta-endorphin-like immunoreactivity in extracts of the fetal bovine pancreas. Column chromatographic characterizations of a high-molecular-weight immunoreactive species.
Acid-ethanol extracts of fetal bovine pancrease were examined for the presence of beta-endorphin-like immunoreactivity. Gel-filtration analyses revealed the presence of a major large-molecular-weight beta-endorphin immunoreactive species of approximately 20K delta. This molecular form maintained its size upon resubmission to gel filtration in the presence of 6 M guanidine hydrochloride, separated from the bulk of the glucagon immunoreactivity upon ion-exchange chromatography, showed proportional dilution in the beta-endorphin radioimmunoassay, and interacted in a biospecific manner with Concanavalin-A-Sepharose.
Animals↗
Glycoprotein-like large glucagon immunoreactive species in extracts of the fetal bovine pancreas.
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.
Animals↗
Glucagon from the bovine fetal pancreas: chromatographic and electrophoretic characterizations of high molecular weight immunoreactive species.
Fetal bovine pancreas was extracted for glucagon using (A) ethanol-Hcl after trichloroacetic acid (TCA) treatment of the pancreas, (B) ethanol-HCl and (C) urea-acetic acid. Fractionation of the acetic acid soluble proteins vi Sephadex G-50 columns yielded glucagon immunoreactivity in the void volume, high molecular weight glucagon immunoreactivities (HMW-IRGs), "proglucagon" (approximately equal to 9 K delta), and true glucagon (3.5 K delta) regions. HMW-IRGs were obtainable using all three methods of extraction. The material obtained from the ethanol-HCl-TCA method appeared stable on Sephadex G-100 (1 M acetic acid) rechromatography. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis analysis showed immunoreactive species corresponding to approximately 40 K delta and approximately 12 K delta. HMW-IRGs did not bind to concanavalin A (Con A)-agarose. SDS-polyacrylamide gel electrophoresis of the Con A-agarose filtered IRG again showed a major immunoreactive peak of approximately 40 K delta. Dose-response RIA studies indicated that the HMW-IRGs from both the gel filtration and SDS-polyacrylamide gel experiments were immunochemically indistinguishable from glucagon. HMW-IRGs bind to antiglucagon antibody agarose, further indicating their reactivity towards glucagon antibodies. When HMW-IRGs are incubated with guanidinium hydrochloride and gel filtered in the same system, a significant fraction of HMW-IRG (representing up to 25% of the total IRG analysed) was found to resist disruption. Our data support the contention that a significant portion of the HMW-IRGs (molecular weight greater than 20 K delta) extracted from fetal bovine pancreas are composed of glucagon covalently linked to larger protein unit(s).
Animals↗
[Paleopathology in Peru].
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History, Ancient↗