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Biomedical subjects

J Markese

Publications and source records attributed to J Markese.

6 recordsLinked to original sources
PubMed1979

A structurally abnormal insulin causing human diabetes.

Insulin isolated from the pancreas of a diabetic patient with fasting hyperinsulinaemia showed decreased activity in binding to cell membrane insulin receptors and in stimulating cellular 2-deoxyglucose transport and glucose oxidation. Chemical studies suggest that the isolated hormone is a mixture of normal insulin and an abnormal variant which contains a leucine for phenylalanine substitution at position 24 or 25 of the insulin B-chain.

Amino Acid Sequence↗
PubMed1977

High titer glucagon antisera.

Antibody titers in rabbits immunized with glucagon conjugated to albumin using difluorodinitrobenzene rose rapidly. Under conditions of immunoassay, less than 2 nl of serum from two of four animals and approximately 4 nl from the other two was required to bind 50% of the 10 pg of [125I]iodoglucagon 100 days after immunization. The dissociation constants of the two higher titer antisera for glucagon were approximately 1 x 10(-10)M, and their binding capacities for the hormone, about 50 mug/ml. Competitive binding assays showed that neither of these antisera cross-reacts with the glucagon-like, immunoreactive peptides extracted from intestine to greater than 2.5%. In contrast, hens produced antisera which were reactive with the intestinal material and which bound only 0.3 mug of glucagon per ml. There were no consistent differences, however, in the abilities of specific and non-specific antisera to react with selected fragments of pancreatic glucagon.

Animals↗
PubMed1976

Glucagon-like and insulin-like hormones of the insect neurosecretory system.

Aqueous extracts of corpus cardiacum-corpus allatum complexes of the adult tobacco hornworm Manduca sexta produced both glycogenolysis and hypoglycaemia when injected into the larval form of the same species. Application of specific radioimmuno assays to similar extracts showed also that these gland complexes contain both glucagon-like and insulin-like peptides. Further, the partially purified immunoreactive peptides had the expected biological activities. The former decreased the glycogen content of the fatbody and the latter the circulating trehalose levels in recipient animals. These results suggest the existence of hormones in these invertebrates having both biological and structural similarities to vertebrate insulin and glucagon.

Animals↗