Zobrazeno 1 - 10
of 54
pro vyhledávání: '"Villamarín JA"'
Publikováno v:
Archives of Biochemistry and Biophysics. 359:57-62
Cytosolic extracts from the posterior adductor muscle of the bivalve mollusk Mytilus galloprovincialis contain significant amounts of both cGMP-binding and cGMP-stimulated protein kinase activities. However, photoaffinity labeling with 8-azido-[ 32 P
Autor:
Ramiro Barcia, Maria Dolores Vazquez Illanes, Izaskun Ibarguren, Juan Ignacio Ramos-Martinez, Villamarín Ja
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 104:641-647
1. 1. Fru-2,6-P2 plays an important modulating role in the glycolysis/gluconeogenesis of sessile marine molluscs, indicating by its content the change in both the flow direction and the glycogen reserves. 2. 2. PFK-1 is activated, while FBPase-1 is i
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 104:255-258
1. 1. The fructose-1,6-bisphosphatase (FBPase-1) of the sea mussel mantle Mytilus galloprovincialis Lmk, was phosphorylated by cAMP-dependent protein kinase. 2. 2. The phosphorylation produced an increase in the V max , a decrease in the value of the
Autor:
Juan Ignacio Ramos-Martinez, Izaskun Ibarguren, M. D. Vazquez-Illanes, Ramiro Barcia, Villamarín Ja
Publikováno v:
Marine Biology. 112:277-281
6-phosphofructo-2-kinase (PFK-2) from the mantle of the sea musselMytilus galloprovincialis Lmk, collected from the Ria de Arosa (NW Spain) in 1990, was purified 550-fold by extraction and sequential affinity chromatography on Affi-gel Blue and ATP-a
Autor:
Villamarín Ja, Juan Ignacio Ramos-Martinez, Ramiro Barcia, Maria Dolores Vasquez-Illanes, Izaskun Ibarguren
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 100:635-639
1. 1. The enzyme fructose-1,6-bisphosphatase was purified from the mantle of the sea mussel Mytilus galloprovincialis Lmk. The purified enzyme showed a single band in SDS-polyacrylamide gel electrophoresis. The mol. wt and subunit mol. wt of the enzy
Publikováno v:
Journal of Experimental Zoology. 255:272-279
Phosphofructokinase (PFK) from the mantle of Mytilus galloprovincialis Lmk. was purified 302-fold with a yield of 27%. The enzyme proved to be a 340,000-dalton oligomer comprising four identical 85,000-dalton subunits. Like other phosphofructokinases
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 95:531-534
The dependence of the initial rate on the concentration of MgATP 2− and fructose-6-phosphate, its behaviour with the alternative substrates MgGTP 2− and MgITP 2- and the inhibition patterns by its products, suggest that the reaction catalysed by
Publikováno v:
Archives of biochemistry and biophysics. 353(2)
The phosphorylation state of phosphofructokinase from the mantle tissue of the facultative anaerobe mollusk Mytilus galloprovincialis was determined by a back-phosphorylation technique. The incubation of intact mantle tissue with 8-bromoadenosine 3':
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Akademický článek
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