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 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 the dihaem cytochrome c4 from the bacterium Azotobacter vinelandii

1984 ◽  
Vol 222 (1) ◽  
pp. 217-227 ◽  
Author(s):  
R P Ambler ◽  
M Daniel ◽  
K Melis ◽  
C D Stout
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Azotobacter Vinelandii ◽  
Cysteine Residues ◽  
British Library ◽  
Single Polypeptide Chain ◽  
Cytochromes C ◽  
Single Polypeptide

An amino acid sequence is proposed for the cytochrome c4 from the bacterium Azotobacter vinelandii strain OP. It is a single polypeptide chain of 190 residues, with two sets of haem-attachment cysteine residues at positions 14/17 and 119/122. Proteins with similar sequences are also present in denitrifying pseudomonads. There is similarity in sequence between the two halves of the cytochrome c4 molecule, and each half also shows similarity to the sequences of certain monohaem cytochromes c isolated from organisms that are not obviously closely related to A. vinelandii. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50125 (17 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment.

scholarly journals The amino acid sequence of cytochrome c-555 from the methane-oxidizing bacterium Methylococcus capsulatus

1986 ◽  
Vol 233 (2) ◽  
pp. 333-337 ◽  
Author(s):  
R P Ambler ◽  
H Dalton ◽  
T E Meyer ◽  
R G Bartsch ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Cysteine Residues ◽  
British Library ◽  
Methylococcus Capsulatus ◽  
Methionine Residue ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of the cytochrome c-555 from the obligate methanotroph Methylococcus capsulatus strain Bath (N.C.I.B. 11132) was determined. It is a single polypeptide chain of 96 residues, binding a haem group through the cysteine residues at positions 19 and 22, and the only methionine residue is a position 59. The sequence does not closely resemble that of any other cytochrome c that has yet been characterized. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50131 (12 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment.

scholarly journals The amino acid sequence of cytochrome f from the brown alga Alaria esculenta (L.) Grev

1975 ◽  
Vol 149 (1) ◽  
pp. 271-279 ◽  
Author(s):  
M V Laycock
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Brown Alga ◽  
Polypeptide Chain ◽  
Cytochrome F ◽  
British Library ◽  
Amino Acid Residues ◽  
Single Polypeptide Chain ◽  
Alaria Esculenta ◽  
Single Polypeptide

Cytochrome f was isolated from the brown alga Alaria esculenta and the amino acid sequence was determined. The native haemoprotein has a molecular weight of 9800 and consists of a single polypeptide chain of 86 amino acid residues with a haem group bonded to cysteine residues at positions 14 and 17. The N-terminus is not acetylated and no methylated lysines were found. Sequences of three other algal cytochromes f were compared with that of Alaria and 22 out of 92 positions were common to the four sequences. One-half of these conserved sites occur between positions 49 and 63. Detailed evidence for the amino acid sequence of Alaria cytochrome has been deposited as Supplementary Publication SUP 50048 (6 pages) 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. (1975) 145, 5.

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 plastocyanin from French bean (Phaseolus vulgaris)

1974 ◽  
Vol 143 (3) ◽  
pp. 691-701 ◽  
Author(s):  
P. R. Milne ◽  
J. R. E. Wells ◽  
R. P. Ambler
Keyword(s):  
Amino Acid ◽  
Phaseolus Vulgaris ◽  
Amino Acid Sequence ◽  
French Bean ◽  
British Library ◽  
Single Polypeptide Chain ◽  
Unicellular Green Alga ◽  
Green Alga Chlorella ◽  
Lending Library ◽  
Single Polypeptide

The amino acid sequence of the plastocyanin from French bean (Phaseolus vulgaris) was determined. The protein consists of a single polypeptide chain of 99 residues, and the sequence was determined by characterization of CNBr, tryptic, chymotryptic and thermolysin peptides. When the sequence is compared with that from the plastocyanin of the unicellular green alga Chlorella fusca, the French-bean protein shows the deletion of the N-terminal residue, a two residue insertion and 53 identical residues. Detailed evidence for the sequence of the protein has been deposited as Supplementary Publication SUP 50037 (16pp., 1 microfiche) at the British Library (Lending Division) (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

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.

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