نتایج جستجو برای: milk clotting enzyme mce
تعداد نتایج: 317972 فیلتر نتایج به سال:
Lactadherin, a glycoprotein of the milk-fat globule membrane, contains tandem C domains with homology to discoidin-type lectins and to membrane-binding domains of blood-clotting factors V and VIII. We asked whether the structural homology confers the capacity to compete for the membrane-binding sites of factor VIII and factor V and to function as an anticoagulant. Our results indicate that lact...
crude enzyme (beta-galactosidase) extract (cee) was produced by lactobacillus ssp. bulgaricus chr hansen lb-12 and was applied in sterile milk which had been processed through ultra high temperature method (uht milk), for hydrolyzing lactose. lactosehydrolyzed milk was also produced by a pure and commercially available betagalactosidase (maxilact). optimum quantities of cee and maxilact enz...
In the structural-based mutagenesis of Mucor pusillus pepsin (MPP), understanding how κ-casein interacts with MPP is a great challenge for us to explore. Chymosin-sensitive peptide is the key domain of κ-casein that regulates milk clotting through the specific proteolytic cleavage of its peptide bond (Phe¹⁰⁵-Met¹⁰⁶) by MPP to produce insoluble para-κ-casein. Here, we built the model of this lar...
Drummond, Margaret C. (Emory University, Atlanta, Ga.) and Morris Tager. Enzymatic activities associated with clotting of fibrinogen by staphylocoagulase and coagulase-reacting factor and their inhibition by diisopropylfluorophosphate. J. Bacteriol. 83:975-980. 1962.-The chemical mechanism of fibrinogen clotting by staphylocoagulase and its plasma factor (CRF) involves a preliminary stage of pr...
Chicken pepsinogen was incubated at pH2.5 with pepstatin. The zymogen activated itself by a sequential mechanism and an intact peptide derived from residues 1-26 in the protein was released in the first step. This peptide was found to inhibit the milk-clotting activities of pig and chicken pepsins and calf chymosin but to different extents.
Lactadherin, a glycoprotein of the milk-fat globule membrane, contains tandem C domains with homology to discoidin-type lectins and to membrane-binding domains of blood-clotting factors V and VIII. We asked whether the structural homology confers the capacity to compete for the membrane-binding sites of factor VIII and factor V and to function as an anticoagulant. Our results indicate that lact...
نمودار تعداد نتایج جستجو در هر سال
با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید