[Physiology of the hydrophobic domain].
The role of the hydrophobic part in the functioning of some amphipathic enterocyte enzymes has been studied in various animal species (fish, mammals, insects). Kinetic (Km, Vmax, pHopt) and regulatory properties of membrane, detergent and protease forms of carbohydrases, alkaline phosphatase and alanine aminopeptidase were compared. All the species under study showed significant differences among these forms of enzymes. The data obtained demonstrate the important role of the hydrophobic anchor in forming both catalytic and regulatory properties of enzymes.
Khiutter
G Iu
GIu
Egorova
V V
VV
Nikitina
A A
AA
D000469:Alkaline Phosphatase / Q000378:metabolism; D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D018826:CD13 Antigens; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004285:Dogs; D005399:Fishes; D006026:Glycoside Hydrolases / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000201:enzymology*; D008968:Molecular Conformation; D011817:Rabbits; D013045:Species Specificity; D013237:Stereoisomerism; D014337:Trout
D006867:Hydrolases; D000469:Alkaline Phosphatase; D006026:Glycoside Hydrolases; C019822:carbohydrase; D000626:Aminopeptidases; D018826:CD13 Antigens
Fiziologiia gidrofobnogo domena.