Arylisothiocyanate modification of sarcoplasmic Ca2+-stimulated ATPase

Journal Article · Wed Apr 01 04:00:00 EST 1981 · J. Bioenerg. Biomembr.; (United States)

DOI:https://doi.org/10.1007/BF00744748· OSTI ID:5615317

Sigrist, H; Zahler, P

The related probes phenylisothiocyanate and p-sulfophenylisothiocyanate possess comparable reactivity with nucleophiles but are dissimilar in their solubility characteristics. The reagents are utilized to topologically characterize the sites of covalent interaction with the Ca2/sup +/-timulated ATPase of sarcoplasmic reticulum membranes. The hydrophobic probe phenylisothiocyanate binds covalently to the membrane-integrated protein. The extent of covalent interaction of this probe is reduced to a limited level of label incorporation by either preincubation with p-sulfophenylisothiocyanate or by exposing the labeled protein to alkaline reductive conditions. With respect to the chemical nature a dual interaction of phenylisothiocyanate is postulated. Phenylisothiocyanate modifies the Ca2/sup +/-ATPase hydrophobically. In addition, aqueous-exposed nucleophiles (cysteine thiols) interact with both arylisothiocyanates. Inhibition of the Ca2/sup +/-stimulated ATPase activity is effected by either probe.

• OSTI ID: 5615317
• Journal Information: J. Bioenerg. Biomembr.; (United States), Journal Name: J. Bioenerg. Biomembr.; (United States) Vol. 13:1-2; ISSN JBBID
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ACID ANHYDRASES
ANTITHYROID DRUGS
ATP-ASE
BIOCHEMICAL REACTION KINETICS
CALCIUM IONS
CARBONIC ACID DERIVATIVES
CHARGED PARTICLES
DRUGS
ENZYMES
HORMONE ANTAGONISTS
HYDROLASES
IONS
KINETICS
MEMBRANES
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PHOSPHOHYDROLASES
REACTION KINETICS
SOLUBILITY
THIOCYANATES