Zobrazeno 1 - 10
of 46
pro vyhledávání: '"H M, RANNEY"'
Publikováno v:
Hemoglobin. 18:221-226
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eaf8aabbbe3f83604ba90186004adac6
https://doi.org/10.3109/03630269409043622
https://doi.org/10.3109/03630269409043622
Autor:
H. M. Ranney
Publikováno v:
Science (New York, N.Y.). 267(5204)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::053f941ac7eda9994de1384db64f19fd
https://pubmed.ncbi.nlm.nih.gov/17808136
https://pubmed.ncbi.nlm.nih.gov/17808136
Autor:
R L, Nagel, H M, Ranney
Publikováno v:
Seminars in hematology. 27(4)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::684405478304a74ee988762a88272468
https://pubmed.ncbi.nlm.nih.gov/2255919
https://pubmed.ncbi.nlm.nih.gov/2255919
Autor:
H M, Ranney
Publikováno v:
Seminars in hematology. 27(4)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e2aa26df7f4871e86020bbaef378fbf4
https://pubmed.ncbi.nlm.nih.gov/2255916
https://pubmed.ncbi.nlm.nih.gov/2255916
Autor:
H M, Anderson, H M, Ranney
Publikováno v:
Seminars in hematology. 27(3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8455a772015de532f9ee5ad079514845
https://pubmed.ncbi.nlm.nih.gov/2197727
https://pubmed.ncbi.nlm.nih.gov/2197727
Publikováno v:
Proceedings of the National Academy of Sciences. 78:65-68
The interactions of hemoglobin S with the erythrocyte membrane were compared with the corresponding interactions of hemoglobin A by measuring in both steady-state and kinetic experiments the quenching of the fluorescence of a probe embedded in erythr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::302d58bb1bddef277bf0f7d19ab47862
https://doi.org/10.1073/pnas.78.1.65
https://doi.org/10.1073/pnas.78.1.65
Autor:
V S Sharma, H M Ranney
Publikováno v:
Journal of Biological Chemistry. 253:6467-6472
The reaction between nitrosylhemoglobin and an excess of deoxymyoglobin has been used to study the kinetics of ligand dissociation from Hb4(NO)4 and Hb4(no)1 species. The kinetics of the dissociation of the first NO molecule from Hb4(no)4 was studied
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b62942670fae0ee44d2e7da44a733b40
https://doi.org/10.1016/s0021-9258(19)46956-1
https://doi.org/10.1016/s0021-9258(19)46956-1
Publikováno v:
Scopus-Elsevier
Rabbit hemoglobin shows significantly lower affinity for CO than does human hemoglobin (Hb A). The overall ligand combination and dissociation rate constants reveal, however, only small differences between Hb A rabbit Hb; this is mainly due to the fa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b64956121e853dfff796e908216a9c08
https://doi.org/10.1016/s0021-9258(19)70712-1
https://doi.org/10.1016/s0021-9258(19)70712-1
Publikováno v:
Proceedings of the National Academy of Sciences. 75:3747-3750
The kinetic data on model compounds of hemoglobin indicate that in oxyderivatives ligand dissociation rates are sensitive to the "tension" exerted by the proximal base on the metal-to-ligand bond; the corresponding rates for carboxy derivatives are n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43cb7ee97a81b403b8bfe0330d7df123
https://doi.org/10.1073/pnas.75.8.3747
https://doi.org/10.1073/pnas.75.8.3747