scholarly journals The primary structure of the calcium ion-transporting adenosine triphosphatase protein of rabbit skeletal sarcoplasmic reticulum:peptides derived from digestion with cyanogen bromide, and the sequences of three long extramembranous segments

1980 ◽  
Vol 191 (3) ◽  
pp. 899-899
Keyword(s):  
Primary Structure ◽  
Calcium Ion ◽  
Adenosine Triphosphatase ◽  
Cyanogen Bromide

scholarly journals The primary structure of the calcium ion-transporting adenosine triphosphatase protein of rabbit skeletal sarcoplasmic reticulum. Peptides derived from digestion with cyanogen bromide, and the sequences of three long extramembranous segments

1980 ◽  
Vol 187 (3) ◽  
pp. 591-616 ◽  
Author(s):  
G Allen ◽  
B J Trinnaman ◽  
N M Green
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Primary Structure ◽  
Calcium Ion ◽  
Adenosine Triphosphatase ◽  
Cyanogen Bromide ◽  
Secondary Structures ◽  
British Library ◽  
Isolation And Characterization ◽  
Tryptophan Residues

The isolation and characterization of the soluble peptides from the CNBr digest of the calcium ion-transporting adenosine triphosphatase protein of rabbit skeletal sarcoplasmic reticulum are described. The 562 unique residues of the protein were placed in sequences. The remaining part of the protein (about 500 residues) yielded long hydrophobic sequences that contained all but one of the tryptophan residues of the protein and that were probably derived largely from the intramembranous parts of the protein. Three long stretches of primary structure, constituting half of the protein, have been reconstructed from the information presented here together with the sequences found in peptides from other digests of the protein. The secondary structures of these sequences have been predicted. A model for the primary structure of the protein is presented and the implications discussed. Details of the isolation of peptides are contained in Supplementary Publication, SUP 50105 (29 pages), which has been deposited with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

scholarly journals Primary structure of the calcium ion-transporting adenosine triphosphatase of rabbit skeletal sarcoplasmic reticulum. Soluble peptides from the α-chymotryptic digest of the carboxymethylated protein

1980 ◽  
Vol 187 (3) ◽  
pp. 565-575 ◽  
Author(s):  
G Allen
Keyword(s):  
Amino Acid ◽  
Sarcoplasmic Reticulum ◽  
Primary Structure ◽  
Calcium Ion ◽  
Adenosine Triphosphatase ◽  
British Library ◽  
Tryptic Peptides

The isolation of the soluble peptides from the chymotryptic digest of the calcium-transporting ATPase of rabbit skeletal sarcoplasmic reticulum is described. These peptides were partially sequenced and the information obtained was used to align tryptic peptides of the protein and to confirm sequences within the tryptic peptides. Details of the isolation of some peptides and the amino acid analyses of the peptides are given in Supplementary Publication SUP 50103 (10 pages), which has been deposited with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

scholarly journals Primary structure of the calcium ion-transporting adenosine triphosphatase from rabbit skeletal sarcoplasmic reticulum. Some peptic, thermolytic, tryptic and staphylococcal-proteinase peptides

1980 ◽  
Vol 187 (3) ◽  
pp. 577-589 ◽  
Author(s):  
G Allen ◽  
R C Bottomley ◽  
B J Trinnaman
Keyword(s):  
Protein Structure ◽  
Sarcoplasmic Reticulum ◽  
Lipid Bilayer ◽  
Primary Structure ◽  
Calcium Ion ◽  
Adenosine Triphosphatase ◽  
British Library

The soluble peptides from the peptic digest of the reduced S-carboxymethylated 3-carboxypropionylated adenosine triphosphatase protein have been isolated and most of their structures have been determined. About 397 residues of the protein were represented in these peptides. The reduced S-carboxymethylated protein was digested with thermolysin, and peptides containing arginine or carboxymethylcysteine were isolated and characterized. Some peptides isolated from tryptic and staphylococcal-proteinase digests of the protein are described. The information contained within the structures of these peptides has been used to reconstruct long stretches of the sequence of the ATPase protein that constitute most of the protein structure external to the lipid bilayer (Allen, Trinnaman and Green (1980) Biochem. J. 187, 591-616). The details of some of the chromatographic steps used in the isolation of the peptides and the properties of the peptides are contained in Supplementary Publication SUP 50104 (45 pages), which has been deposited with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

scholarly journals Primary structures of cysteine-containing peptides from the calcium ion-transporting adenosine triphosphatase of rabbit sarcoplasmic reticulum

1978 ◽  
Vol 173 (2) ◽  
pp. 393-402 ◽  
Author(s):  
G Allen ◽  
N M Green
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Primary Structure ◽  
Calcium Ion ◽  
Adenosine Triphosphatase ◽  
Preliminary Investigation ◽  
British Library ◽  
Native Protein ◽  
Tryptic Peptides ◽  
Derivatives Of

A preliminary investigation of the primary structure of the Ca(2+-transporting ATPase (adenosine triphosphatase) protein of rabbit skeletal-muscle sarcoplasmic reticulum is reported. The preparation of derivatives of delipidated protein in a form suitable for sequence analysis is described. Tryptic peptides containing S-carboxymethylcysteine residues were isolated from the reduced carboxymethylated protein, and their sequences were partially determined. The results are consistent with mol.wt. about 105000 for the polypeptide, and the absence of extended repeated lengths of sequence. The distribution of tryptophan and cysteine residues between large, aggregated peptides and soluble tryptic peptides shows that these residues are concentrated in different regions of the primary structure. This observation agrees with other evidence that these residues are, on the whole, widely separated in the native protein. The details of the procedures used to isolate the peptides, and the evidence for the determination of their sequences, are given Supplementary Publication SUP 50085 (30 pages), which has been deposited at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem.J. (1978) 169, 5.

Primary structure of human intrinsic factor: progress report on cyanogen bromide fragmentation

1978 ◽  
Vol 38 (7) ◽  
pp. 649-653 ◽  
Author(s):  
Ebba Nexø ◽  
Henrik Olesen ◽  
Marianne Rye Hansen ◽  
Ditlef Bucher ◽  
Johannes Thomsen
Keyword(s):  
Primary Structure ◽  
Cyanogen Bromide ◽  
Intrinsic Factor ◽  
Progress Report
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