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)

We recently published the primary structure and inhibition data of the barley grain aspartic proteinase (HvAP, Hordeum vulgare aspartic proteinase) which revealed similarity to mammalian cathepsin D and yeast aspartic proteinase A. Here we present evidence, based on Km and kcat values for the enzyme as well as on its cleavage sites in haemoglobin, the insulin B-chain, glucagon and melittin, that the similarity extends to its hydrolytic specificity. Like the animal and microbial aspartic proteinases, HvAP preferentially cleaves peptide bonds between amino acid residues with large hydrophobic side chains. The narrow hydrolytic specificity of HvAP suggests that plant aspartic proteinases may perform regulatory functions by limited proteolysis.
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PMID:Hydrolytic specificity of the barley grain aspartic proteinase. 776 75

We investigated whether bovine milk constituents influenced glucagon-like peptide (GLP)-2 secretion and intestinal growth in suckling rats. Male Sprague-Dawley rats (14 d old) received i.g. infusions of a milk protein fraction, a lactose solution, or the cream fraction of milk. The serum concentration of GLP-2, but not GLP-1, markedly increased in rats administered milk protein compared with those given the lactose solution or the cream fraction from 60 to 120 min after administration. In another experiment, both casein (CN) and whey protein isolate stimulated GLP-2 secretion at 120 min after administration, but soy protein and ovalbumin did not. Stimulation of GLP-2 secretion by several milk proteins was similar, including alpha-CN, alpha-lactalbumin (alpha-La), and beta-lactoglobulin, in a separate experiment. A hydrolysate of alpha-La obtained by incubation with protease A extracted from Aspergillus oryzae (LaHPA) caused almost twice the GLP-2 release due to intact alpha-La and other alpha-La hydrolysates. Free amino acid concentrations and molecular size distributions did not differ among alpha-La hydrolysates, including LaHPA. In rat pups reared with milk formulae containing alpha-La or LaHPA, LaHPA significantly promoted small intestinal elongation and increased the number of crypt epithelial cells compared with a formula containing intact alpha-La. LaHPA administration also increased the maltase:lactase activity ratio, a marker of maturation of the intestinal mucosa. In conclusion, milk proteins stimulate GLP-2 secretion and contribute to growth and maturation of the small intestine in suckling rats.
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PMID:alpha-Lactalbumin hydrolysate stimulates glucagon-like peptide-2 secretion and small intestinal growth in suckling rats. 1949 23