Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide.

Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide. Abstract Text:

K Saito-Nakatsuka,T Yamashita,I Kubota,M Kawakita,

Ca2+-Transporting ATPase of rabbit skeletal muscle sarcoplasmic reticulum contains several SH groups which are reactive with N-ethylmaleimide (MalNEt) at pH 7.0. The location of the one which is most reactive with MalNEt (SHN, Kawakita et al. J. Biochem. 87, 609 (1980)) was identified on the amino acid sequence of the ATPase. SHN was labeled by reacting sarcoplasmic reticulum membranes with [14C] MalNEt to a labeling density of 1 mol/mol ATPase. [14C]MalNEt-labeled membranes were digested with thermolysin and 14C-labeled SHN peptides were fractionated by Sephadex LH-20 chromatography to give two major peaks of radioactivity. [14C]-MalNEt-labeled peptides were further purified to homogeneity by C18-reversed phase HPLC. Two radioactive peptides containing modified cysteine (Cys), Leu-Gly-Cys-Thr-Ser and Val-Cys-Lys-Met, were finally obtained in roughly equal amounts and in reasonable recovery. Both of these sequences were found in the amino acid sequence of Ca2+-transporting ATPase (Brandl et al. Cell 44, 597 (1986)), and Cys344 and Cys364 were identified as the targets of MalNEt-modification. Thus, 0.5 mol/mol ATPase of each Cys residue actually reacted rapidly with MalNEt under the conditions leading to SHN-modification. Modification of either one with MalNEt may negatively affect the reactivity of the other. Both of the highly reactive SH groups are located in the neighborhood of Asp351, the phosphorylation site of ATPase.

Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide. Publishing Authors By Initials

K Saito-Nakatsuka,T Yamashita,I Kubota,M Kawakita,

For similar sulfhydryl compounds research abstracts see: sulfhydryl compounds research

PUBMED ID PMID:

MEDLINE DATE:

Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 101

Page Numbers: 365-76

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 1987

Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide. Keywords Mesh Terms:

KEYWORDS: Sulfhydryl Compounds

MESH TERMS: metabolism

Chemical & Substance for Abstract: Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase I Location of a group which is most reactive with N-ethylmaleimide Related Publications

• Affinity labeling of the ATP-binding site of Ca2+-transporting ATPase of sarcoplasmic reticulum by adenosine triphosphopyridoxal: identification of the reactive lysyl residue.
• An improved method of determining free and acetylated polyamines by HPLC involving an enzyme reactor and an electrochemical detector.
• Analysis of the binding sites of Gd3+ on Ca(2+)-transporting ATPase of the sarcoplasmic reticulum through its effects on fluorescence of tryptophan residues and a covalently attached fluorescent probe N-(1-anilinonaphthyl-4)maleimide.
• Ca2(+)-dependent conformational change of the ATP-binding site of Ca2(+)-transporting ATPase of sarcoplasmic reticulum as revealed by an alteration of the target-site specificity of adenosine triphosphopyridoxal.
• Characterization of Gd3+ and Tb3+ binding sites on Ca2+,Mg2+-adenosine triphosphatase of sarcoplasmic reticulum.
• Characterization of the Na+/H(+)-antiporter of bovine renal cortex and its immunoaffinity purification in a reconstitutively active form.
• Chemical modification and fluorescence labeling study of Ca2+,Mg2+-adenosine triphosphatase of sarcoplasmic reticulum using iodoacetamide and its N-substituted derivatives.
• Conformational aberrance of the sendai virus F0 protein in thapsigargin-treated cells allowing exit from the endoplasmic reticulum but causing arrest at the Golgi complex.
• Conformational change of Ca2+,Mg2+-adenosine triphosphatase of sarcoplasmic reticulum upon binding of Ca2+ and adenyl-5'-yl-imidodiphosphate as detected by trypsin sensitivity analysis.
• Determination of amounts of polyamines excreted in urine: demonstration of N1,N8-diacetylspermidine and N1,N12-diacetylspermine as components commonly occurring in normal human urine.
• Effect of temperature and added ligands on the susceptibility of Ca2+,Mg2+-adenosine triphosphatase of the sarcoplasmic reticulum to trypsin.
• Expression and activity of chimeric molecules between human UDP-galactose transporter and CMP-sialic acid transporter.
• Human UDP-galactose translocator: molecular cloning of a complementary DNA that complements the genetic defect of a mutant cell line deficient in UDP-galactose translocator.
• Indispensability of transmembrane domains of Golgi UDP-galactose transporter as revealed by analysis of genetic defects in UDP-galactose transporter-deficient murine had-1 mutant cell lines and construction of deletion mutants.
• Limited tryptic digestion of Ca2+,Mg2+-adenosine triphosphatase of the sarcoplasmic reticulum: enzymatic properties of A1b + B complex.
• Location of the Ca(2+)-transport site of Ca(2+)-transporting ATPase of the sarcoplasmic reticulum as determined by analysis of paramagnetic interaction between Gd3+ ions bound at the transport site and membrane-embedded nitroxide spin probes.
• Purification of limited tryptic fragments of Ca2+,Mg2+-adenosine triphosphatase of the sarcoplasmic reticulum and identification of conformation-sensitive cleavage sites.
• Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. I. Location of a group which is most reactive with N-ethylmaleimide.
• Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. II. Site of labeling with iodoacetamide and its fluorescent derivative.
• Reconstitution of Na+/H(+)-antiporter of bovine renal brush-border membrane into proteoliposomes and detection of a 110 kDa protein cross-reactive with antibodies against a human Na+/H(+)-antiporter partial peptide in antiport-active fractions after parti
• Sites of labeling with N-(3-pyrene)maleimide on Ca(2+)-transporting ATPase of the sarcoplasmic reticulum.
• Studies on conformational transitions of Ca2+, Mg2+-adenosine triphosphatase of sarcoplasmic reticulum. I. Selective labeling of functionally distinct sulfhydryl groups with conformational probes and evidence for a Ca2+-dependent conformational change.
• Studies on conformational transitions of Ca2+,Mg2+-adenosine triphosphatase of sarcoplasmic reticulum. II. Conformational characteristics of stabilized reaction intermediates as revealed by fluorescent and paramagnetic probes.
• Studies on polypeptide elongation factor from E. coli. I. Crystalline factor G.
• Studies on the respiratory system of Aspergillus oryzae. 3. Properties of mitochondria from mycelia grown in the presence of antimycin A.
• Studies on the respiratory system of Aspergillus oryzae. II. Preparation and some properties of mitochondria from mycelia.
• The target reaction in the antiviral action of mouse interferon against vesicular stomatitis virus multiplication.
• Transport of envelope proteins of Sendai virus, HN and F0, is blocked at different steps by thapsigargin and other perturbants to intracellular Ca2+.
• Two enzyme-linked immunosorbent assay (ELISA) systems for N1,N8-diacetylspermidine and N1,N12-diacetylspermine using monoclonal antibodies.
• Uncoupling of ATP splitting from Ca(2+)-transport in Ca(2+)-transporting ATPase of the sarcoplasmic reticulum as a result of modification by N-(3-pyrene)maleimide: activation of a channel with a specificity for alkaline earth metal ions.