Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Michiaki Morohashi"'
Publikováno v:
Journal of UOEH. 16:277-286
Chimeric proteins consisting of parts from the alpha-subunit of Torpedo californica (Na, K) ATPase (N) and the rabbit sarcoplasmic reticulum Ca-ATPase (C) were expressed in Xenopus oocytes by injecting the respective chimeric cRNA in combination with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2475fc1c94d8920dc48f7f1570adab99
https://doi.org/10.7888/juoeh.16.277
https://doi.org/10.7888/juoeh.16.277
Autor:
Gary C du Moulin, Michiaki Morohashi
Publikováno v:
Materials Science and Engineering: C. 13:15-17
A greater understanding in cell biology now makes it possible to cultivate, expand, and manipulate many kinds of living cells into innovative therapies. Since 1991, the US Food and Drug Administration (USFDA) has been very active in formulating polic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a83432773bad4d8bb26d97b5b0ddc04a
https://doi.org/10.1016/s0928-4931(00)00171-5
https://doi.org/10.1016/s0928-4931(00)00171-5
Publikováno v:
Journal of Comparative Physiology B. 161:69-72
An inhibitory activity to (Na,K)ATPase was found in cell extracts of the brine shrimp, Artemia salina, irrespective of its developmental stages. Organic solvent extraction together with gas chromatographic analysis reveals that the inhibitory activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f631a5efff67062884cc877ba82a4f8
https://doi.org/10.1007/bf00258748
https://doi.org/10.1007/bf00258748
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1021:157-160
Point mutations of Asp-376 of the alpha-subunit of Torpedo californica Na+/K(+)-ATPase (the site of phosphorylation during the catalytic cycle) to Asn, Glu or Thr led to virtual abolishment of Na+/K(+)-ATPase activity and ouabain-binding capacity. Re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d3fb0f2945ed83fed5fa1448e11d57e
https://doi.org/10.1016/0005-2736(90)90028-m
https://doi.org/10.1016/0005-2736(90)90028-m
Publikováno v:
Biochemical and Biophysical Research Communications. 130:221-228
(Na,K)-ATPase from Torpedo californica (electric ray) and Artemia salina (brine shrimp) was labeled with flourescein 5′-isothiocyanate (FITC) with concomitant loss of activity. Both inactivation and binding were inhibited in the presence of ATP. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02cc18adf496650a24492d0a89e7ae16
https://doi.org/10.1016/0006-291x(85)90405-x
https://doi.org/10.1016/0006-291x(85)90405-x
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 821:115-120
Purified dog kidney (Na+ + K+)-ATPase (EC 3.6.1.3) was inactivated with high concentrations of 2-mercaptoethanol at 50-55 degrees C. The inactivation was prevented by NaCl or KCl, with KCl being more effective than NaCl (the former ion being about on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::807fa3d70f19a918a95d2cc44c956fcc
https://doi.org/10.1016/0005-2736(85)90161-0
https://doi.org/10.1016/0005-2736(85)90161-0
Publikováno v:
Journal of biochemistry. 103(6)
The membrane bound (Na,K)-ATPase prepared from Artemia salina nauplii was solubilized with a zwitterionic detergent, 3[3(cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), and then purified on a Bio-Gel A-1.5 m column in the presence of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0a68d5ffb07af05a00e4a02ca706dd9
https://pubmed.ncbi.nlm.nih.gov/2844745
https://pubmed.ncbi.nlm.nih.gov/2844745