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Biomedical subjects

A E Kitabchi

Publications and source records attributed to A E Kitabchi.

At least 109 records · Page 6Linked to original sources
PubMed1975

Diabetes mellitus in fluctuant hearing loss.

1. In 161 consecutive cases of fluctuant hearing loss and 13 control cases of other causes of deafness, patients were examined for their ability to metabolize a 100 gm. oral dose of glucose. 2. The plasma glucose level in response to the oral dose of glucose was measured at hourly intervals for three hours. 3. Insulin and proinsulin levels were measured in 46 cases of fluctuant hearing loss and in 13 control cases. 4. None of the control group showed borderline or diabetic tolerance curves. 5. Fourteen per cent of the patients with fluctuant hearing loss had borderline glucose intolerance curves and 19 per cent showed diabetic glucose tolerance curves. 6. In patients whose insulin and proinsulin levels were determined, the insulin response to an oral glucose load was typical of adult onset diabetes, i.e., delayed hyperinsulinemia with concomitant hyperglycemia. The hyperinsulinemia was not associated with hyperproinsulinemia. 7. We conclude that in patients with fluctuant hearing loss there is a significantly higher incidence of borderline or diabetic glucose tolerance than in the "control deafness" or "normal population" group.

Adult↗
PubMed1975

Hormonal control of glucose metabolism.

Glucose homeostasis is accomplished through two major hormones, glucagon and insulin. These hormones, of course, must work in concert with other permissive hormones such as glucocorticoids and catecholamines to bring about a multiplicity of physiological processes such as gluconeogenesis, glycolysis, lipolysis, and proteolysis that maintain the organism's biochemical integrity.

Blood Glucose↗
PubMed1972

Purification of insulin-specific protease by affinity chromatography.

A single enzyme that proteolytically degrades insulin was isolated from rat skeletal muscle. This enzyme was purified 1000-fold by a series of steps, including affinity chromatography on insulin bound to agarose at the NH(2)-terminal phenylalanine of the B chain. Insulin linked to agarose at the B-29 lysine residue did not bind the enzyme and, therefore, was not suitable for purification procedures. Insulin linked at the phenylalanine residue was a substrate for the enzyme and was degraded by it; insulin attached to agarose at the lysine residue was not degraded by the enzyme. The purified enzyme preparation yielded one major band on polyacrylamide gel electrophoresis, and elution of this area of the gel yielded insulin-degrading activity. The purified enzyme degraded insulin but not proinsulin, with a K(m) for insulin of 22 nM and a K(i) for proinsulin of 40 nM. The enzyme is sulfhydryl-dependent, with a physiological pH optimum.

Animals↗