Zobrazeno 1 - 10
of 146
pro vyhledávání: '"R, Cassoly"'
Publikováno v:
European Journal of Biochemistry. 219:503-511
We have previously shown that in human or pig whole erythrocytes, only a single 71-kDa polypeptide cross-reacts with the affinity-purified antibody to pig platelet caldesmon (der Terrossian et al., 1989). In the present paper, we demonstrate that thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07bd8cd3afe945a87bb085d18e005454
https://doi.org/10.1111/j.1432-1033.1994.tb19965.x
https://doi.org/10.1111/j.1432-1033.1994.tb19965.x
Publikováno v:
European journal of cell biology. 54(1)
The plasma membrane of nucleated erythrocytes contains a microtubular marginal band which appears to be associated with the plasma membrane skeleton. In this report, we identify two families of cytoskeletal proteins which may be involved in such an a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eee2a47a26e5eac84c7b739a1ad772e9
https://pubmed.ncbi.nlm.nih.gov/2032540
https://pubmed.ncbi.nlm.nih.gov/2032540
Publikováno v:
AIP Conference Proceedings.
The role of the microtubular marginal band (MT‐MB) in the mature nucleated chicken erythrocyte is still not well understood. We show here, in stopped flow experiments, that the kinetics of swelling of the chicken red blood cells, subsequent to a fa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d87cb0a69431a9abed11df468a078e53
https://doi.org/10.1063/1.40586
https://doi.org/10.1063/1.40586
Publikováno v:
Journal of Biological Chemistry. 254:11351-11356
The binding of various linear and branched chain alkylisocyanides to soybean leghemoglobin has been studied with respect to association and dissociation kinetics and the results compared with those obtained in parallel on sperm whale and horse heart
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0cfca09c7c1837907449e9c750a8046b
https://doi.org/10.1016/s0021-9258(19)86492-x
https://doi.org/10.1016/s0021-9258(19)86492-x
Autor:
J M Salhany, R Cassoly
Publikováno v:
Journal of Biological Chemistry. 264:1399-1404
Hemoglobin binds to the cytoplasmic domain of band 3 protein (CDB3) at physiologic pH and ionic strength in an oxygen-linked fashion, with deoxyhemoglobin having the higher affinity. The evidence in the literature suggests functional communication be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc7a0b8802752858c29e0ec28fb2e0c1
https://doi.org/10.1016/s0021-9258(18)94201-8
https://doi.org/10.1016/s0021-9258(18)94201-8
Autor:
R Cassoly
Publikováno v:
Journal of Biological Chemistry. 253:3602-3606
It has been recently demonstrated that some nitrosyl hemoglobin derivatives have different optical spectrum according to the nature of their quaternary structure (Cassoly, R. (1974) C. R. Seances Acad. Sci., Paris 278, 1417-1420; Salhany, J. M., Ogaw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::31869d3755e7d8011a141de687f6ce62
https://doi.org/10.1016/s0021-9258(17)34844-5
https://doi.org/10.1016/s0021-9258(17)34844-5
Autor:
R Cassoly
Publikováno v:
Journal of Biological Chemistry. 258:3859-3864
The association of the isolated cytoplasmic fragment of band 3 protein with human hemoglobin was studied by rate zonal centrifugation in sucrose density gradients, by quenching of fragment fluorescence by hemoglobin, and by flash photolysis of carbon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2cd3574778db476ac1eed5bc818bdb8d
https://doi.org/10.1016/s0021-9258(18)32746-7
https://doi.org/10.1016/s0021-9258(18)32746-7
Autor:
R. Cassoly
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 168:370-373
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3d4f5908a06ea024ce19d62ae32f096
https://doi.org/10.1016/0005-2795(68)90163-3
https://doi.org/10.1016/0005-2795(68)90163-3
Autor:
R. Banerjee, R. Cassoly
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 133:545-556
The preparation and partial characterization of an unusual hemoglobin derivative, containing only 2 hemes per 4 chains, are described. The compound has been isolated in small yield from a solution of methemoglobin having undergone a partial loss of h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8adf464990da9add8aafcae86883371e
https://doi.org/10.1016/0005-2795(67)90559-4
https://doi.org/10.1016/0005-2795(67)90559-4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 133:557-567
Semi -hemoglobin, an abnormal but stable di-heme derivative obtained from human hemoglobin, has been characterized and its main properties have been studied. It has been shown to have a normal α 2 s 2 composition with its 2 hemes located on the α-c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3eccfd50d14a043cd958736d70f22923
https://doi.org/10.1016/0005-2795(67)90560-0
https://doi.org/10.1016/0005-2795(67)90560-0