Learn More
To understand the mechanical behavior of fast-starting fish, we modeled the pumpkinseed sunfish, Lepomis gibbosus, as a longitudinally-loaded beam that behaves as an elastic column eccentrically-loaded by lateral musculature. Since bending moments are a function of the shape of the body, we used real sunfish to determine, (1) from cross-sections, the(More)
The binding of vanadate and fluorescein isothiocyanate to the Ca2+-transport ATPase of sarcoplasmic reticulum (EC 3.6.1.3) was analyzed. Monovanadate binds to the Ca2+-transport ATPase at a single high affinity site (site 1), that is presumably related to the binding site for inorganic orthophosphate, and to one of the two sites for decavanadate. Binding of(More)
The binding of monovanadate and decavanadate anions to sarcoplasmic reticulum vesicles was measured by equilibrium sedimentation. The affinity of vanadate binding and the molar amount of vanadium (V) bound at equilibrium is much greater with decavanadate than with monovanadate. The binding data can be rationalized in terms of one binding site per ATPase(More)
The existence of small- and large-scale membrane protein clusters, containing dimers, oligomers and hundreds of proteins, respectively, has become widely accepted. However, it is largely unknown whether the internal structure of these formations is dynamic or static. Cell fusion was used to perturb the distribution of existing membrane protein clusters, and(More)
The influence of chemical modification on the morphology of crystalline ATPase aggregates was analyzed in sarcoplasmic reticulum (SR) vesicles. The Ca2+-ATPase forms monomer-type (P1) type crystals in the E1 and dimer-type (P2) crystals in the E2 conformation. The P1 type crystals are induced by Ca2+ or lanthanides; P2 type crystals are observed in(More)
  • 1