Characterization of the properties of ethenoadenosine nucleotides bound or trapped at the active site of myosin subfragment 1

Biochemistry ◽  
1984 ◽  
Vol 23 (17) ◽  
pp. 3994-4002 ◽  
Author(s):  
William J. Perkins ◽  
James A. Wells ◽  
Ralph G. Yount
Keyword(s):  
Active Site ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

scholarly journals The Role of Magnesium in Binding of the Nucleotide Polyphosphate Chain to the Active Site of Myosin Subfragment-1

1983 ◽  
Vol 134 (2) ◽  
pp. 197-204 ◽  
Author(s):  
Marcus C. SCHAUB ◽  
John G. WATTERSON ◽  
Klaus LOTH ◽  
Daniela FOLETTA
Keyword(s):  
Active Site ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

Characterization of Myosin Subfragment-1 of Summer and Winter Silver Carp (Hypophthalmichthys molitrix) Muscle

2012 ◽  
Vol 77 (9) ◽  
pp. C914-C920 ◽  
Author(s):  
Liang Zheng ◽  
Kefeng Yu ◽  
Chunhong Yuan ◽  
Xichang Wang ◽  
Shunsheng Chen ◽  
...  
Keyword(s):  
Silver Carp ◽  
Hypophthalmichthys Molitrix ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

scholarly journals Regulation of the acto·myosin subfragment 1 interaction by troponin/tropomyosin. Evidence for control of a specific isomerization between two acto·myosin subfragment 1 states

1991 ◽  
Vol 279 (3) ◽  
pp. 711-718 ◽  
Author(s):  
D F A McKillop ◽  
M A Geeves
Keyword(s):  
Skeletal Muscle ◽  
Active Site ◽  
Actin Filaments ◽  
Thin Filaments ◽  
Closed State ◽  
Myosin Subfragment ◽  
Actomyosin Interaction ◽  
Binding Isotherms ◽  
Myosin Subfragment 1 ◽  
Site Binding

The co-operative binding of myosin subfragment 1 (S1) to reconstituted skeletal-muscle thin filaments has been examined by monitoring the fluorescence of a pyrene probe on Cys-374 of actin. The degree of co-operativity differs when phosphate, sulphate or ADP are bound to the S1 active site. Binding isotherms have been analysed according to the Geeves & Halsall [(1987) Biophys. J. 52, 215-220] model, which proposed that troponin and tropomyosin effected regulation of the actomyosin interaction by controlling an isomerization of the actomyosin complex. The data support the proposal that seven actin monomers associated with a single tropomyosin molecule act as a co-operative unit that can be in one of two states. In the ‘closed’ state myosin can bind to actin, but the subsequent isomerization is prevented. The isomerization is only allowed after the seven-actin unit is in the ‘open’ form. Ca2+ controls the proportion of actin filaments in the ‘closed’ and ‘open’ forms in the absence of myosin heads. The ratio of ‘closed’ to ‘open’ forms is approx. 50:1 in the absence of Ca2+ and 5:1 in its presence.

scholarly journals Isolation and characterization of circumferential microfilament bundles from retinal pigmented epithelial cells.

1982 ◽  
Vol 95 (1) ◽  
pp. 310-315 ◽  
Author(s):  
K Owaribe ◽  
H Masuda
Keyword(s):  
Epithelial Cells ◽  
Electrophoretic Pattern ◽  
Isolation And Characterization ◽  
Microfilament Bundles ◽  
Myosin Subfragment ◽  
Sds Page ◽  
Myosin Subfragment 1 ◽  
Retinal Pigmented Epithelial Cells ◽  
Large Contraction

Chicken retinal pigmented epithelial cells have circumferential microfilament bundles (CMBs) at the zonula adherens region. We have isolated these CMBs in intact form and characterized them structurally and biochemically. Pigmented epithelia obtained from 11-d-old chick embryos were treated with glycerol and Triton. Then, the epithelia were homogenized by passing them through syringe needles. Many isolated CMBs were found in the homogenate by phase-contrast microscopy. They formed polygons, mostly pentagons and hexagons, or fragments of polygons. Polygons were filled with meshwork structures, i.e. they were polygonal plates. Upon exposure to Mg-ATP, isolated CMBs showed clear and large contraction. The contraction was inhibited by treatment with N-ethylmaleimide-modified myosin subfragment-1. After purification by centrifugation with the density gradient of Percoll, CMBs were analyzed by SDS PAGE. The electrophoretic pattern gave three major components of 200, 55, and 42 kdaltons and several minor components. Electron microscopy showed that the polygons were composed of thick bundles of actin-containing microfilaments, and the meshworks were composed primarily of intermediate filaments.

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