Zobrazeno 1 - 10
of 12
pro vyhledávání: '"L G, Makevnina"'
Publikováno v:
Immunopharmacology. 32:160-162
The specificity of the peptide hydrolyzing action of a highly purified preparation of kininase from Latrodectus Tredecimguttatus venom was studied by the method of TLC on silica gel with the use of various synthetic peptides as substrates. It was sho
Publikováno v:
Vestnik Rossiiskoi akademii meditsinskikh nauk. (12)
The improvement of blood supply in the ischemic brain (post-ischemic cerebral reperfusion), which results from surgical treatment, has been shown to improve the neurological status only in the patients who had no lower baseline levels of kininogens (
Publikováno v:
Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas. 27(8)
1. Total kininogen, high molecular weight kininogen and low molecular weight kininogen were quantitated as bradykinin equivalents in the blood flowing to and from the brain in patients with stenotic and occlusive carotid damage in the course of neuro
Publikováno v:
Agents and actions. Supplements. 38
The initial rates of Lys-bradykinin release by porcine pancreatic kallikrein from rabbit low molecular weight kininogen are found to follow the Michaelis-Menten kinetics with kc = 0.62 sec-1 and Km = 1.93 microM at substrate concentrations 0.3-1.3 mi
Publikováno v:
Biokhimiia (Moscow, Russia). 55(8)
The nature of the bradykinin (BK)-hydrolyzing (kininase) activity of peptidhydrolase isolated from spider (Latr. tredecimguttatus) venom has been studied. It was found that the BKase activity of the enzyme is fully inhibited by organic mercurials (10
Publikováno v:
Biokhimiia (Moscow, Russia). 52(5)
The inhibition of trypsin, human blood plasma kallikrein and porcine pancreatic kallikrein by aprotinin (native and immobilized on carboxymethyl ester of dextran) was investigated. The experimental values of Ki of native and immobilized aprotinin--en
Publikováno v:
Doklady Akademii nauk SSSR. 276(5)
Publikováno v:
Biokhimiia (Moscow, Russia). 50(2)
A highly purified preparation of low molecular weight kininogen (LMrK) was isolated from the plasminogen-free rabbit blood plasma, using chromatography on DEAE-Sepharose CL-6B, gel filtration on Ultrogel AcA 34 and Sephadex G-100 as well as gradient
Publikováno v:
Advances in the biosciences. 17
[Amino acid makeup, structural characteristics and substrate specificity of rabbit plasma kininogen]
Publikováno v:
Biokhimiia (Moscow, Russia). 40(1)
Highly purified kininogen preparation with the activity of 16-18 int. units per mg was isolated from rabbit blood serum. Its molecular weight was estimated to be 54 000 by gel filtration through Sephadex G-200. Leucine was identified as N-terminal am