Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01275 (glucagon)
 26,492 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The specificity of bovine spleen cathepsin B2 has been investigated by means of some natural oligo- and polypeptides, i.e. glucagon, melittin, insulin A and B chain, bradykinin, angiotensin I and II, oxytocin ACTH, clupein and salmin. The enzyme is primarily a carboxypeptidase which hydrolyzes peptide linkages of most amino acids common to proteins. In addition, cathepsin B2 displays amidase and esterase activity without requiring a free carboxyl group. The main pH optimum is between 4 and 5, in some cases higher.
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PMID:On the specificity of bovine spleen cathepsin B2. 1 11

Rat liver was perfused in vitro with Krebs-Henseleit-medium and albumin at 25 degrees C in a recirculating system without hemoglobin over a period of 120 min. The following basic parameters for characterization of isolated liver perfusion were recorded: medium-pO2 prior and after liver passage, flow-rate, pH, and hepatic O2-consumption. Beyond this, concentration of lactate and pyruvate, hepatic glucose production, activity of aspartate-aminotransferase, leucine-aminopeptidase and acylase as well as concentration of K+-ions in the perfusion fluid were measured. In dependence on nutrition state of liver donors (fed or starved rats) the rate of glycogenolysis or rate of lactate-stimulated gluconeogenesis was calculated. The endogenous glycogenolysis can be blocked by an in vivo injection of propranolol. The propranolol-inhibited glycogenolysis can be stimulated by an in vitro glucagon application.
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PMID:[Characterization of the functional state of the in vitro Hb-free perfused rat liver]. 733 31

Glucagon, a peptide hormone produced by alpha-cells of Langerhans islets, is a physiological antagonist of insulin and stimulator of its secretion. In order to improve its bioactivity, we modified its structure at the C-terminus by amidation catalyzed by a recombinant amidase in bacterial cells. The human gene coding for glucagon-gly was PCR amplified using three overlapping primers and cloned together with a rat alpha-amidase gene in plasmid pMGA. Both genes were expressed under control of the strong constitutive promoter of aph and secretion signal melC1 in Streptomyces lividans. With Phenyl-Sepharose 6 FF, Q-Sepharose FF, SP-Sepharose FF chromatographies and HPLC, the peptide was purified to about 93.4% purity. The molecular mass of the peptide is 3.494 kDa as analyzed by MALDI TOF, which agrees with the theoretical mass value of the C-terminal amidated glucagon. The N-terminal sequence of the peptide was also determined, confirming its identity with human glucagon at the N-terminal part. ELISA showed that the purified peptide amide is bioactive in reacting with glucagon antibodies.
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PMID:Expression, purification, and characterization of C-terminal amidated glucagon in Streptomyces lividans. 1860 50