Conformational responses of the tryptic cleavage products of the Ca2+-ATPase of sarcoplasmic reticulum.

This publication has 21 references indexed in Scilit:

• Two-dimensional arrays of proteins in sarcoplasmic reticulum and purified Ca2+-ATPase vesicles treated with vanadate.
  Journal of Biological Chemistry, 1983
• Disruption of energy transduction in sarcoplasmic reticulum by trypsin cleavage of (Ca2++Mg2+)-ATPase
  The Journal of Membrane Biology, 1982
• Identification of a labelled peptide after stoicheiometric reaction of fluorescein isothiocyanate with the Ca²⁺‐dependent adenosine triphosphatase of sarcoplasmic reticulum
  FEBS Letters, 1982
• Modification of the ATP binding site of the Ca²⁺‐ATPase from sarcoplasmic reticulum by fluorescein isothiocyanate
  FEBS Letters, 1981
• Indications for an oligomeric structure and for conformational changes in sarcoplasmic reticulum Ca2+-ATPase labelled selectively with fluorescein
  Biochimica et Biophysica Acta (BBA) - Protein Structure, 1980
• Primary structure of the calcium ion-transporting adenosine triphosphatase from rabbit skeletal sarcoplasmic reticulum. Some peptic, thermolytic, tryptic and staphylococcal-proteinase peptides
  Biochemical Journal, 1980
• Denaturation of the tryptic fragments of the calcium(II) adenosine triphosphatase from sarcoplasmic reticulum by guanidinium hydrochloride
  Biochemistry, 1978
• Mechanism of ATP hydrolysis by sarcoplasmic reticulum and the role of phospholipids.
  Journal of Biological Chemistry, 1976
• A 31‐residue tryptic peptide from the active site of the [Ca⁺⁺]‐transporting adenosine triphosphatase of rabbit sarcoplasmic reticulum
  FEBS Letters, 1976
• PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
  Journal of Biological Chemistry, 1951