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 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.

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 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 The primary structure of the calcium-transporting adenosine triphosphatase of rabbit skeletal sarcoplasmic reticulum. Soluble tryptic peptides from the succinylated carboxymethylated protein

1980 ◽  
Vol 187 (3) ◽  
pp. 545-563 ◽  
Author(s):  
G Allen
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Lipid Bilayer ◽  
Adenosine Triphosphatase ◽  
Succinic Anhydride ◽  
Amino Acid Sequences ◽  
British Library ◽  
Tryptic Peptides ◽  
Hydrophobic Peptides ◽  
Arginine Residues

The isolation and the determination of the amino-acid sequences of the soluble tryptic peptides, derived by cleavage at arginine residues, of the succinylated (3-carboxypropionylated) S-carboxymethylated adenosine triphosphatase protein of rabbit skeletal sarcoplasmic reticulum are described. Treatment of the protein with succinic anhydride gave a derivative that was readily digested with trypsin, yielding two distinct sets of peptides. One set comprises large, relatively hydrophobic, peptides that are highly aggregated (or insoluble) in aqueous solution and that have been identified, by several criteria, with the portion of the protein embedded in the lipid bilayer in the sarcoplasmic reticulum. The second set, which is described here, comprises peptides that have properties typical of those derived from soluble globular proteins and that constitute that part of the protein external to the lipid bilayer. The sequences of these soluble tryptic peptides contain 586 unique residues. Details of the isolation of the peptides and the determination of the sequences are contained in Supplementary Publication SUP 50102 (88 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.

Ca2+-ATPase and function of sarcoplasmic reticulum during cardiac hypertrophy

1991 ◽  
Vol 261 (4) ◽  
pp. L23-L26 ◽  
Author(s):  
Dmitri Levitsky ◽  
Diane De La Bastie ◽  
Ketty Schwartz ◽  
Anne-Marie Lompré
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Cardiac Hypertrophy ◽  
Calcium Ion ◽  
Adenosine Triphosphatase ◽  
State Level ◽  
Calcium Sensitivity ◽  
Left Ventricular ◽  
Pump System ◽  
Messenger Ribonucleic Acid ◽  
And Function

The properties of the calcium pump system of sarcoplasmic reticulum (SR) were studied in a series of 34 rats subjected to cardiac overload and 19 sham-operated animals. Total homogenates of left ventricle were analyzed by measuring the oxalate-supported Ca2+ uptake rate, the steady-state level of the phosphorylated intermediate of Ca2+-adenosine triphosphatase (Ca2+-ATPase) (E-P), and the amount of Ca2+-ATPase mRNA. All three parameters decreased gradually as a function of the relative left ventricular weight increase. The calcium-sensitivity curves showed that the velocity of Ca2+ transport in SR from the hypertrophied heart is diminished at low as well as optimal Ca2+2 concentrations, with the dissociation constant (Kd) value for Ca2+ unchanged from that of the control preparation. Taken together with the results presented in our recent publication (De la Bastie, Levitsky, Mercadier, Marotte, Wisnewsky, Brovkovivh, Schwartz, and Lompré, Circ. Res. 66: 554–564, 1990), these data strongly indicate that differences in the Ca2+ pump activities of SR from normal and hypertrophied rat hearts are due to quantitative rather than qualitative changes of the Ca2+-ATPase protein. calcium ion uptake; calcium ion adenosine triphosphatase messenger ribonucleic acid; cardiac hypertrophy; monoclonal antibody

scholarly journals The amino acid sequence of the α chain of the major haemoglobin of the rat (Rattus norvegicus)

1975 ◽  
Vol 149 (1) ◽  
pp. 259-269 ◽  
Author(s):  
C G Chua ◽  
R W Carrell ◽  
B H Howard
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rattus Norvegicus ◽  
Peptide Mapping ◽  
Cysteine Residue ◽  
British Library ◽  
Peptide Fragments ◽  
Partial Amino Acid Sequence ◽  
Tryptic Peptides ◽  
Α Chain

1. A partial amino acid sequence of the α chain from the rat (Wistar, Rattus norvegicus) major haemoglobin is reported. The soluble tryptic peptides prepared from aminoethylated α-globin were separated by peptide ‘mapping’. Sequencing of the tryptic peptides was carried out by the dansyl-Edman method and by the overlapping of smaller peptide fragments derived from secondary enzymic digestion. The insoluble ‘core’ peptides were further digested with chymotrypsin, thermolysin and pepsin to give smaller soluble peptides for sequencing. The tryptic peptides were ordered on the basis of their homology with the corresponding peptides of human α chain. 2. The proposed sequence is compared with that obtained by using an automated sequencer [Garrick et al. (1975) Biochem. J.149, 245-258]. The differences in sequence resulting from the two methods are discussed. 3. It is suggested that the externally situated cysteine (residue 13) is responsible for the observed inhibition of crystallization of rat haemoglobin at alkaline pH. 4. Detailed evidence for the sequence has been deposited as Supplementary Publication SUP 50047 (9 pages) at the British Library (Linding Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from which copies can be obtained on the terms given in Biochem. J. (1975) 145, 5.

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