Zobrazeno 1 - 10
of 167
pro vyhledávání: '"K. Bárány"'
Publikováno v:
Annals of the New York Academy of Sciences. 138:360-366
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a85a6129871cf6860995a0a6fb08b69c
https://doi.org/10.1111/j.1749-6632.1966.tb41177.x
https://doi.org/10.1111/j.1749-6632.1966.tb41177.x
Akademický článek
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Publikováno v:
Clinical Chemistry. 30:2063-2068
Phosphorylation of the 20 000-Da light chain of myosin in functionally different porcine carotid arteries was determined, with use of two-dimensional gel electrophoresis. Stretching arteries to 1.7 times their resting length resulted in maximal phosp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5191df902cd48a32cacea6385c80f12c
https://doi.org/10.1093/clinchem/30.12.2063
https://doi.org/10.1093/clinchem/30.12.2063
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 491:387-397
About 6–7% of the total proteins from trichloroacetic acid-washed and freeze-dried frog muscle could be extracted with acid chloroform/methanol. Three of these proteins were found to be phosphorylated in the live frog. They were purified to apparen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb00ebad64beb8fa02ae4e4da111fa02
https://doi.org/10.1016/0005-2795(77)90281-1
https://doi.org/10.1016/0005-2795(77)90281-1
Autor:
S.T. Sayers, K. Bárány
Publikováno v:
FEBS Letters. 154:305-310
The phosphorylation of myosin P-light chain was determined during the contraction cycle of turtle heart beating 5--8 times/min at 5 degrees C. The hearts were freeze-clamped either in systole or diastole, then homogenized and washed in strong acids i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f11cb29be500891f4cdd8e015f3cc88
https://doi.org/10.1016/0014-5793(83)80172-0
https://doi.org/10.1016/0014-5793(83)80172-0
Publikováno v:
Journal of Supramolecular Structure. 3:125-140
The reactivity of myosin to [14C]-labeled N-ethylmaleimide ([14C]NEM) or to tritium was determined in functionally different frog muscles. The incorporation of [14C]NEM into myosin decreased during isotonic or isometric contractions, as compared to r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a00077604048aa81307abb02e26600ee
https://doi.org/10.1002/jss.400030205
https://doi.org/10.1002/jss.400030205
Publikováno v:
Biochimica et Biophysica Acta : BBA
The inhibition of the actin-L-myosin interaction by urea 1. 1. With increasing concentration, urea transforms actomyosin ATPase of washed myofibrils and of purified actomyosin gels into L-myosin ATPase. This transformation is completed as soon as the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4418bd17cef9aa83d2f25db0114f427
https://doi.org/10.1016/0006-3002(60)91455-4
https://doi.org/10.1016/0006-3002(60)91455-4
Publikováno v:
Journal of Biological Chemistry. 252:4752-4754
Changes in the 32P content of proteins due to muscle contraction were investigated, using muscles dissected from liver frogs injected with [32P]orthophosphate. The only significant change found was in the radioactivity of the 18,000-dalton light chai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f483f3275639e099cc21368dadbfeeb5
https://doi.org/10.1016/s0021-9258(17)40117-7
https://doi.org/10.1016/s0021-9258(17)40117-7
Publikováno v:
The Journal of biological chemistry. 255(13)
The myosin light chain of intact arterial smooth muscle displayed a cyclic phosphorylation-dephosphorylation and rephosphorylation in consort with contraction, followed by relaxation, followed by a second contraction of the muscle. Application of pha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c7b2f9476d870e4ce609443d58aaf8e8
https://pubmed.ncbi.nlm.nih.gov/6771267
https://pubmed.ncbi.nlm.nih.gov/6771267
Publikováno v:
Federation proceedings. 42(1)
Phosphorylation of myosin light chain was compared in various muscles. In 32P-labeled chicken anterior latissimus dorsi and posterior latissimus dorsi the [32P]phosphate content of the 19,000-dalton and 18,000-dalton light chains, respectively, was 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::abe03f9f4aa1708edb8bee8bbb5b8769
https://pubmed.ncbi.nlm.nih.gov/6848376
https://pubmed.ncbi.nlm.nih.gov/6848376