scholarly journals The amino acid sequence of plastocyanin from Vicia faba L. (broad bean)

1974 ◽  
Vol 141 (3) ◽  
pp. 835-843 ◽  
Author(s):  
John A. M. Ramshaw ◽  
Michael D. Scawen ◽  
Donald Boulter
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Polypeptide Chain ◽  
Broad Bean ◽  
Phenyl Isothiocyanate ◽  
Single Polypeptide Chain ◽  
Vicia Faba L ◽  
Single Polypeptide ◽  
Degradation Of Peptides

The amino acid sequence of plastocyanin from broad bean was determined. It consists of a single polypeptide chain of 99 residues. The sequence was determined by using a Beckman 890C sequencer and by dansyl–phenyl isothiocyanate analysis of peptides obtained by the enzymic cleavage of purified cyanogen bromide fragments. Some parts of the sequence depend on the results of Edman degradation of peptides for which amino acid analyses were not obtained. The evidence for one overlap is not strong.

scholarly journals Chymotryptic inhibitor I from potatoes. The amino acid sequence of subunit A*

1974 ◽  
Vol 137 (1) ◽  
pp. 101-112 ◽  
Author(s):  
M. Richardson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Polypeptide Chain ◽  
Proteinase Inhibitors ◽  
Dilute Acid ◽  
Subunit A ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of subunit A of the potato chymotryptic inhibitor I was determined. The sequence was deduced from analysis of fragments and peptides derived from the protein by cleavage with cyanogen bromide, N-bromosuccinimide and dilute acid, and by digestion with trypsin, thermolysin, pepsin and papain. The molecule consists of a single polypeptide chain of 84 residues, which contains two homologous regions each of 13 amino acids. The protein does not appear to be homologous with any other known proteinase inhibitors.

scholarly journals The amino acid sequence of plastocyanin from Cucurbita pepo L. (vegetable marrow)

1974 ◽  
Vol 143 (2) ◽  
pp. 257-264 ◽  
Author(s):  
Michael D. Scawen ◽  
Donald Boulter
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phenyl Isothiocyanate ◽  
Amino Acid Residues ◽  
Higher Plant ◽  
Single Polypeptide Chain ◽  
Vegetable Marrow ◽  
Single Polypeptide ◽  
Phylogenetic Affinities ◽  
Good Agreement

The amino acid sequence of plastocyanin from marrow was determined. It consists of a single polypeptide chain of mol.wt. 10284 containing 99 amino acid residues. The sequence was determined by using a Beckman 890C automatic sequencer and by dansyl–phenyl isothiocyanate analysis of peptides obtained by the enzymic digestion of purified CNBr fragments. The sequence is in good agreement with the amino acid composition, except that fewer residues of glutamic acid were found in the sequence than were suggested by the composition. Evidence for histidine-37 was weaker than for the rest of the sequence. A ‘tree’ of phylogenetic affinities was constructed by using several higher-plant plastocyanin sequences.

scholarly journals The amino acid sequence of plastocyanin from Solanum tuberosum L. (potato)

1974 ◽  
Vol 139 (3) ◽  
pp. 583-592 ◽  
Author(s):  
John A. M. Ramshaw ◽  
Michael D. Scawen ◽  
Christopher J. Bailey ◽  
Donald Boulter
Keyword(s):  
Molecular Weight ◽  
Solanum Tuberosum ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Solanum Tuberosum L ◽  
Chlorella Fusca ◽  
Considerable Similarity ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of plastocyanin from potato was determined. It consists of a single polypeptide chain of 99 residues, of molecular weight 10332. The sequence was determined by using a Beckman 890c sequencer and by dansyl–Edman analysis of peptides derived from purified CNBr fragments. The sequence shows considerable similarity with that of Chlorella fusca, and also with the C-terminal region of bacterial azurins.

scholarly journals Evidence for the amino acid sequence of porcine pancreatic elastase

1973 ◽  
Vol 131 (4) ◽  
pp. 643-675 ◽  
Author(s):  
David M. Shotton ◽  
Brian S. Hartley
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Pancreatic Elastase ◽  
Single Polypeptide Chain ◽  
Chemical Studies ◽  
Lending Library ◽  
Porcine Pancreatic Elastase ◽  
Single Polypeptide

The preparation and purification of tryptic peptides from aminoethylated Dip-elastase and [14C]carboxymethylated Dip-elastase, and of peptic peptides from native elastase is described. A summary of the results of chemical studies used to elucidate the amino acid sequence of these peptides is presented. Full details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50016 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 1–20. These results, together with those from previously published papers, are used to establish the complete amino acid sequence of elastase, which is a single polypeptide chain of 240 residues, molecular weight 25900, containing four disulphide bridges.

The Amino Acid Sequence of Cytochrome c-553 from the Chrysophycean Alga Monochrysis lutheri

1972 ◽  
Vol 50 (12) ◽  
pp. 1311-1325 ◽  
Author(s):  
M. V. Laycock
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Photosynthetic Apparatus ◽  
Amino Acid Residues ◽  
Unicellular Alga ◽  
Electron Carrier ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of cytochrome c-553, an electron carrier in the photosynthetic apparatus of the unicellular alga Monochrysis lutheri, has been determined. The protein consists of a single polypeptide chain of 83 amino acid residues. The sequence shows homology with mitochondrial cytochrome c at each end of the chain. The N-terminal glycine is not acetylated and corresponds to position 1 of mammalian cytochrome c when the cysteine residues of the two proteins are aligned.

scholarly journals The amino acid sequence of ferredoxin from Triticum aestivum (wheat)

1979 ◽  
Vol 179 (2) ◽  
pp. 373-378 ◽  
Author(s):  
I Takruri ◽  
D Boulter
Keyword(s):  
Triticum Aestivum ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Plant Type ◽  
Considerable Similarity ◽  
Single Polypeptide Chain ◽  
N Terminus ◽  
Cnbr Cleavage ◽  
Single Polypeptide

The amino acid sequence of the ferredoxin of Triticum aestivum (wheat) was determined by using a Beckman 890C sequencer in combination with the dansyl–phenylisothiocyanate method to characterize peptides obtained by tryptic, chymotryptic and thermolytic digestion of CNBr-cleavage fragments. The molecule consists of a single polypeptide chain of 97 residues and has an unblocked N-terminus. It shows considerable similarity to other plant-type ferredoxins.

scholarly journals The amino acid sequence of ferredoxin from Brassica napus (rape)

1980 ◽  
Vol 185 (1) ◽  
pp. 239-243 ◽  
Author(s):  
I Takruri ◽  
D Boulter
Keyword(s):  
Amino Acid ◽  
Brassica Napus ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Plant Type ◽  
Single Polypeptide Chain ◽  
N Terminus ◽  
Single Polypeptide

The amino acid sequence of the ferredoxin of Brassica napus was determined by using a Beckman 890C sequencer in combination with the characterization of peptides obtained by tryptic and chymotryptic digestion of the protein; some peptides were subdigested with thermolysin. The molecule consists of a single polypeptide chain of 96 amino acid residues and has an unblocked N-terminus. The primary structure shows considerable similarity with other plant-type ferredoxins.

scholarly journals The amino acid sequence of Staphylococcus aureus penicillinase

1975 ◽  
Vol 151 (2) ◽  
pp. 197-218 ◽  
Author(s):  
R P Ambler
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Preliminary Report ◽  
Polypeptide Chain ◽  
Aureus Strain ◽  
British Library ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of the penicillinase (penicillin amido-β-lactamhydrolase, EC 3.5.2.6) from Staphylococcus aureus strain PC1 was determined. The protein consists of a single polypeptide chain of 257 residues, and the sequence was determined by characterization of tryptic, chymotryptic, peptic and CNBr peptides, with some additional evidence from thermolysin and S. aureus proteinase peptides. A mistake in the preliminary report of the sequence is corrected; residues 113-116 are now thought to be -Lys-Lys-Val-Lys- rather than -Lys-Val-Lys-Lys-. Detailed evidence for the amino acid sequence has been deposited as Supplementary Publication SUP 50056 (91 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.

scholarly journals The amino acid sequence of plastocyanin from spinach. (Spinacia oleracea L.)

1975 ◽  
Vol 147 (2) ◽  
pp. 343-349 ◽  
Author(s):  
M D Scawen ◽  
J A Ramshaw ◽  
D Boulter
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Spinacia Oleracea ◽  
Sedimentation Equilibrium ◽  
Phenyl Isothiocyanate ◽  
Single Polypeptide Chain ◽  
Spinacia Oleracea L ◽  
Methionine Residues ◽  
Single Polypeptide

The amino acid sequence of spinach (Spinacia oleracea L.) plastocyanin was determined. It consists of a single polypeptide chain of 99 residues and has a sequence molecular weight of 10415. The sequence was determined by using a Beckman 890C automatic sequencer and by the dansyl--phenyl isothiocyanate analysis of peptides obtained by the enzymic digestion of purified CNBr fragments. Overlap through the two methionine residues was not shown. Sedimentation equilibrium in the ultracentrifuge gave a molecular weight for spinach plastocyanin of about 9000, in contrast with the value of 21000 reported previously by Katoh et al. (1962).

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