Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Robert Cardinaud"'
Autor:
Robert Cardinaud
Publikováno v:
European Journal of Biochemistry. 122:527-533
Using precisely monitored proteolytic digestion conditions rabbit fast skeletal muscle myosin could be selectively modified in different ways. A myosin isozyme with a 20-kDa alkali light chain 1 (A1) could be obtained by digesting with papain in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66dc37473fd515e3968f35b26a2d4765
https://doi.org/10.1111/j.1432-1033.1982.tb06469.x
https://doi.org/10.1111/j.1432-1033.1982.tb06469.x
Publikováno v:
FEBS Letters. 369:255-259
The functional significance of myosin light chains in vertebrate striated muscle is an issue of interest and myosin species selectivity modified by papain or trypsin in their LC1 and LC2 light chains are potentially useful for further investigation.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc792399a28adefa06b07aedc905b399
https://doi.org/10.1016/0014-5793(95)00743-s
https://doi.org/10.1016/0014-5793(95)00743-s
Publikováno v:
European journal of biochemistry. 216(1)
The proteolytic susceptibilities of specific sites in the LC1 and LC2 N-termini were modulated by ionic strength in myosin (a species able to form filaments) but not in S1. (a) In the presence of Ca2+ or Mg2+, the proteolytic susceptibility (apparent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3689d5a29f9c0246e0fc3833ed8e213
https://pubmed.ncbi.nlm.nih.gov/8365420
https://pubmed.ncbi.nlm.nih.gov/8365420
Publikováno v:
Biochimie. 74(12)
We selectively modified the LC1 and LC2 N-terminus as an approach to understand the function of skeletal myosin light chains and their possible implication in some diseases. Three new myosin isoforms were thus created, namely: myosin-[(P)LC1'], myosi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::615e3e3f0bbedcd13b8f917cf72f9ee0
https://pubmed.ncbi.nlm.nih.gov/1292616
https://pubmed.ncbi.nlm.nih.gov/1292616
Autor:
Jean J. Leger, Patrick Eldin, Martine Le Cunff, Dominique Mornet, B. Cornillon, I Frangoise Pons, Anne-Marie Cathiard, I Robert Cardinaud, Jocelyne Leger, Monique Anoal, Jean-Pierre Liautard
Publikováno v:
Journal of Muscle Research and Cell Motility
Journal of Muscle Research and Cell Motility, Springer Verlag, 1992, 13 (3), pp.329-340. ⟨10.1007/bf01766461⟩
Journal of Muscle Research and Cell Motility, Springer Verlag, 1992, 13 (3), pp.329-340. ⟨10.1007/bf01766461⟩
Five monoclonal antibodies that react with different regions of myosin light chain 1 from human ventricular myocardial muscle were used to obtain information on interactions between the light chain 1 and heavy chains and generally on the tertiary str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9f088dfe7d4b659133aeaea7a28fa9d
https://hal.archives-ouvertes.fr/hal-02438891
https://hal.archives-ouvertes.fr/hal-02438891
Autor:
Robert Cardinaud, Charles Danzin
Publikováno v:
European Journal of Biochemistry. 62:365-372
Kinetic studies were carried out in order to investigate the enzymic mechanism of a 215-fold-purified purine(pyrimidine) nucleoside: purine(pyrimidine) deoxyribosyl transferase fraction from Lactobacillus helveticus. A variety of natural deoxyribonuc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5331316ea77aed97afe2757597a827b9
https://doi.org/10.1111/j.1432-1033.1976.tb10168.x
https://doi.org/10.1111/j.1432-1033.1976.tb10168.x
Publikováno v:
European Journal of Biochemistry. 54:515-520
A series of purine bases and analogues were tested as substrates for trans-N-deoxyribosylase (EC 2.4.2.6). It was observed that the pyrimidine ring and its substituents on positions 1, 2 and 6, are of minor importance. On the other hand only a few mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53b704b4b3232d9ffff2bb385d628398
https://doi.org/10.1111/j.1432-1033.1975.tb04164.x
https://doi.org/10.1111/j.1432-1033.1975.tb04164.x
Autor:
Robert Cardinaud, José Holguin
Publikováno v:
European Journal of Biochemistry. 54:505-514
trans-N-Deoxyribosylase (EC 2.4.2.6) is usually considered as a single protein catalyzing indifferently the transfer of the deoxyribosyl moiety to and from a purine or a pyrimidine base. Affinity chromatography of an extract from Lactobacillus helvet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b58b09c513b05ac073b8c524770b3b60
https://doi.org/10.1111/j.1432-1033.1975.tb04163.x
https://doi.org/10.1111/j.1432-1033.1975.tb04163.x
Autor:
Robert Cardinaud, Charles Danzin
Publikováno v:
European Journal of Biochemistry. 48:255-262
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e80f598c9b5695b0202da38cfa25d838
https://doi.org/10.1111/j.1432-1033.1974.tb03763.x
https://doi.org/10.1111/j.1432-1033.1974.tb03763.x
Publikováno v:
Journal of the American Chemical Society. 77:934-936
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e8e5a52043c5fdbf92b6aa71b9916783
https://doi.org/10.1021/ja01609a040
https://doi.org/10.1021/ja01609a040