Zobrazeno 1 - 9
of 9
pro vyhledávání: '"A I, Gorodinskiĭ"'
Publikováno v:
Fiziologicheskii zhurnal imeni I.M. Sechenova. 80(1)
Autor:
S A, Dambinova, Iu V, Bobryshev, A I, Gorodinskiĭ, M N, Margulis, A O, Nikitin, E A, Orlova, I Iu, Pavlov, A Iu, Savinov
Publikováno v:
Zhurnal evoliutsionnoi biokhimii i fiziologii. 28(2)
The kinetics of [3H]-L-glutamate binding to brain synaptic membranes (SM) and to glutamate-binding proteins (GBP) was determined with agonist and monoclonal antibodies (MAbs). It was revealed, that rat and human brain GBP have individual protein comp
Publikováno v:
Biokhimiia (Moscow, Russia). 56(9)
Solubilization of the total membrane fraction of human platelets in a 2% solution of sodium deoxycholate and subsequent affinity chromatography on glutamate agarose resulted in two protein fractions possessing a glutamate-binding activity. As can be
Autor:
S A, Dambinova, A I, Gorodinskiĭ
Publikováno v:
Biulleten' eksperimental'noi biologii i meditsiny. 94(12)
Specific binding of 3H-L-glutamate to synaptic membranes isolated from the cerebral cortex and hippocamp of Wistar and Krushinsky-Molodkina (KM) rats examined both in a quiet awake state and after audiogenic seizures was compared. The dissociation co
Publikováno v:
Fiziologicheskii zhurnal SSSR imeni I. M. Sechenova. 70(7)
The transport and selective functions of the glutamate-binding proteins of the rat brain cortex synaptic membranes, were studied. The data on kinetics of absorption of the ions 22Na+, 86Rb+ and 45Ca++ by the membrane vesicles and liposomes containing
Publikováno v:
Biokhimiia (Moscow, Russia). 52(10)
The kinetics of 3H-L-glutamate binding to human brain synaptic membranes revealed the existence of one type of binding sites with Kd and Vmax comparable with those for freshly isolated rat brain membranes. The fraction of glutamate-binding proteins (
Publikováno v:
Biokhimiia (Moscow, Russia). 53(5)
The total membrane fraction of human platelets was found to contain high affinity sites of L-[3H]glutamic acid binding (Kd = 100 nM, Bmax = 1.06 pmol/mg protein). The pH optimum for binding is at pH approximately 6.9 Na+ (1-150 mM) inhibit glutamate
Autor:
S A, Dambinova, A I, Gorodinskiĭ
Publikováno v:
Biokhimiia (Moscow, Russia). 49(1)
The binding of L-[3H]glutamate to rat cerebral cortex synaptic membranes was investigated. Two types of binding sites, a Na+-independent (Kd = 140-160 nm; Bmax = 3.8-4.5 pmol-mg of protein) and a Na+-dependent (Kd = 2.0 microM; Bmax = 45-50 pmol/mg o
Autor:
A I, Gorodinskiĭ, S A, Dambinova
Publikováno v:
Biulleten' eksperimental'noi biologii i meditsiny. 102(9)
The endogenous factor that inhibited 3H-L-glutamate specific binding (FIB) was isolated from the aqueous extract of the crude mitochondrial fraction of the rat cerebral cortex homogenate and partially purified. The purification procedure involved sev