Zobrazeno 1 - 10
of 79
pro vyhledávání: '"Gad Avigad"'
Publikováno v:
Biochemistry and molecular biology international. 40(2)
Incubation of rabbit skeletal myosin with 1 to 3 mM D-glucose 6-phosphate over a period of several hours resulted in the inhibition of the K(+)- and actin activated-ATPase activities. Substrate ATP (0.5-3 mM final concentration) protected the myosin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53d3c984c3ce12f1fdd3ab5e62ec1ab6
https://pubmed.ncbi.nlm.nih.gov/8896749
https://pubmed.ncbi.nlm.nih.gov/8896749
Publikováno v:
Journal of Bacteriology. 118:1051-1058
The accumulation of 5-keto- d -fructose (5KF) by Gluconobacter cerinus grown on d -fructose in unbuffered medium was shown to be optimal at pH 4.0 after cell growth ceased. During the exponential phase of growth or at neutral pH after the onset of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cabddd5e354b8bf7a8a2eeda12a07c2
https://doi.org/10.1128/jb.118.3.1051-1058.1974
https://doi.org/10.1128/jb.118.3.1051-1058.1974
Autor:
Gad Avigad
Publikováno v:
Analytical Biochemistry. 86:443-449
Alcohol and lactic dehydrogenases were covalently bound to concanavalin A. The conjugates obtained retained their ability to bind glycoprotein as well as to carry out NAD + -oxidoreduction in the presence of the appropriate substrates. The dual capac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74365b55e8c7fd050e352017c6f294e2
https://doi.org/10.1016/0003-2697(78)90767-4
https://doi.org/10.1016/0003-2697(78)90767-4
Publikováno v:
Journal of Molecular Biology. 203:495-505
Exposure of rat tail tendon to a reducing sugar results in covalent attachment of the sugar to collagen, a process termed glycation, and leads to the formation of stable intermolecular cross-links. We have used X-ray diffraction to study the changes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b47acb113dd2364342bc1ce26e98b8f6
https://doi.org/10.1016/0022-2836(88)90015-0
https://doi.org/10.1016/0022-2836(88)90015-0
Autor:
Gad Avigad
Publikováno v:
Analytical Letters. 17:371-384
Tissues or cells are extracted in mildly alkaline solutions and reduced by sodium-borohydride. The fructose 6-phosphate released from the intact D-fructose 2,6-bisphosphate by gentle acid hydrolysis is determined fluorimetrically in a coupled enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad03b62d1519e88d1c75ea237283e082
https://doi.org/10.1080/00032718408069084
https://doi.org/10.1080/00032718408069084
Autor:
Moshe Kalina, Gad Avigad
Publikováno v:
FEMS Microbiology Letters. 6:111-114
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::825e6644175cfb2d9e454834b14040c3
https://doi.org/10.1111/j.1574-6968.1979.tb04289.x
https://doi.org/10.1111/j.1574-6968.1979.tb04289.x
Autor:
Gad Avigad
Publikováno v:
Analytical Biochemistry. 86:470-476
A galactose oxidase (EC 1.1.3.9); NADH-peroxidase (EC 1.11.1.1) coupled assay system is used for the estimation of galactose oxidase activity. Spectrophotometric measurement of NADH consumption yields direct quantitative value of enzymic activity or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ee397100f4b3717e6653421025ee06c
https://doi.org/10.1016/0003-2697(78)90771-6
https://doi.org/10.1016/0003-2697(78)90771-6
Publikováno v:
Journal of Biological Chemistry. 263:17650-17657
Incubation of tail tendon from a young rat in solutions containing D-ribose resulted in attachment of the monosaccharide to collagen and subsequent cross-link formation at a rate much faster than found for glucose. The collagen rapidly became resista
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c18d5c92add7d800664aadae11ed15d
https://doi.org/10.1016/s0021-9258(19)77886-7
https://doi.org/10.1016/s0021-9258(19)77886-7
Publikováno v:
Journal of Molecular Biology. 89:651-662
cis,cis-Muconate cycloisomerase (cis,cis-muconate lactonizing enzyme, EC 5.5.1.1.) was purified in crystalline form from Pseudomonas putida. Ultracentrifugation studies, as well as gel filtration chromatography and electrophoresis, indicate that the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e5e4800ba182127e2c2792d51c31290
https://doi.org/10.1016/0022-2836(74)90042-4
https://doi.org/10.1016/0022-2836(74)90042-4