Zobrazeno 1 - 10
of 19
pro vyhledávání: '"David R. Kominz"'
Publikováno v:
Biochemistry. 14:2718-2725
When stoichiometric amounts of tropomyosin (TM) are bound to F-actin in the presence of 2 mM ATP, the MG2+-activated acto-heavy meromyosin (HMM) ATPase is inhibited by about 60% in 5 mM MgCl2-30 mM KCl. If the concentration of MgCl2 is reduced to 1 m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e4ebcc4107e49d483249407a4319f5a6
https://doi.org/10.1021/bi00683a025
https://doi.org/10.1021/bi00683a025
Publikováno v:
Archives of Biochemistry and Biophysics. 49:276-282
The full amino acid composition of bovine prothrombin has been measured by using ion-exchange chromatography. In addition, other methods were used for the estimation of tyrosine, tryptophan, phenylalanine, and amide ammonia. Cysteine-cystine were est
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d415384f75270a9b0a1f6d99e93edf3a
https://doi.org/10.1016/0003-9861(54)90198-8
https://doi.org/10.1016/0003-9861(54)90198-8
Publikováno v:
Biochemical and Biophysical Research Communications. 21:210-214
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e95719f77f712a0f791a61700e284962
https://doi.org/10.1016/0006-291x(65)90273-1
https://doi.org/10.1016/0006-291x(65)90273-1
Autor:
David R. Kominz
Publikováno v:
Biochemistry. 9:1792-1801
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60ab79afdd4709554425b0fc3739293b
https://doi.org/10.1021/bi00810a019
https://doi.org/10.1021/bi00810a019
Autor:
David R. Kominz, Koscak Maruyama
Publikováno v:
The Journal of Biochemistry. 65:465-470
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6765de821a142af192257082ac30376c
https://doi.org/10.1093/oxfordjournals.jbchem.a129035
https://doi.org/10.1093/oxfordjournals.jbchem.a129035
Autor:
David R. Kominz
Publikováno v:
Biochimica et Biophysica Acta. 51:456-463
An ultracentrifugal study has been made on myosin treated with methylmercuric hydroxide. 1. 1. Myosin is transformed by tritration of its -SH groups with methylmerucuric hydroxide to a faster-sedimenting product. This occurs in the same range of meth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8f303be197a6d0ae858b44ef7c57b82
https://doi.org/10.1016/0006-3002(61)90601-1
https://doi.org/10.1016/0006-3002(61)90601-1
Publikováno v:
Archives of Biochemistry and Biophysics. 79:191-199
1. 1. Treatment with 0.1 M Na 2 CO 3 releases from myosin a protein of about 29,000 molecular weight, which seems to be closely related to the material released from myosin by concentrated urea. 2. 2. The amino acid composition is presented. A relati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd3f78498889ef03aa91924d54b16bba
https://doi.org/10.1016/0003-9861(59)90395-9
https://doi.org/10.1016/0003-9861(59)90395-9
Autor:
K. Maruyama, David R. Kominz
Publikováno v:
Archives of Biochemistry and Biophysics. 90:52-56
Treatment with heavy-metal cyanides at alkaline pH splits both rabbit and crayfish myosins into three portions. The fraction salting out at 38–42% ammonium sulfate saturation has a sedimentation rate of about 3 S . The amino acid compositions of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca296b7275da07a444ec6daa76399919
https://doi.org/10.1016/0003-9861(60)90610-x
https://doi.org/10.1016/0003-9861(60)90610-x
Publikováno v:
Biochimica et Biophysica Acta. 63:106-116
1. 1. Purified tropomyosin has been prepared from adult and larval stages of the blowfly, Phormia regina ; purified myosin and actin have been prepared from the adult stage only. Special procedures were required in the preparation of all three protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc3d2ab50f1fc97c6b2022e6fcf60cf1
https://doi.org/10.1016/0006-3002(62)90343-8
https://doi.org/10.1016/0006-3002(62)90343-8
Autor:
David R. Kominz
Publikováno v:
Archives of Biochemistry and Biophysics. 115:583-592
It is confirmed that the presence of native tropomyosin is required in order for the removal of Ca ++ to cause inhibition of the Mg ++ -activated ATPase of actomyosin and acto-heavy-meromyosin. Native tropomyosin is present in routinely purified samp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ffce85c4048f27a7833254399f16b31
https://doi.org/10.1016/0003-9861(66)90078-6
https://doi.org/10.1016/0003-9861(66)90078-6