[Digestion of Luliberine analogues containing D-alanine residue by human gastric juice].
The digestion of surphagone and other luliberine analogues containing residues of D-amino acids by human gastric juice was studied. By means of chromatography and mass spectrometry, these peptides were shown to undergo hydrolysis of the bond formed by D-Ala at the P-1 position, and this hydrolysis was shown to be catalyzed by gastricsin rather than pepsin A. Gastricsin was assumed to be a highly specific protease. The results are in a good agreement with the concept of conformational specificity of proteases towards the natural oligopeptides.
Mirgorodskaia
O A
OA
Savel'eva
N V
NV
Simankova
A N
AN
Shevchenko
A A
AA
Aleksandrov
S L
SL
D000409:Alanine / Q000378:metabolism*; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D005750:Gastric Juice / Q000737:chemistry* / Q000378:metabolism; D007987:Gonadotropin-Releasing Hormone / Q000031:analogs & derivatives* / Q000378:metabolism*; D006728:Hormones / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D013058:Mass Spectrometry; D010434:Pepsin A / Q000737:chemistry; D011487:Protein Conformation
D006728:Hormones; D007987:Gonadotropin-Releasing Hormone; C010661:surfagon; D010434:Pepsin A; C020557:gastricsin; D000409:Alanine
Rasshcheplenie zheludochnym sokom cheloveka analogov liuliberina, soderzhashchich ostatok D-alanina.