Purification and partial characterization of an exo-β-glucanase from the yeast Kluyveromyces aestuarii

1977 ◽  
Vol 55 (9) ◽  
pp. 1001-1006 ◽  
Author(s):  
Marc-André Lachance ◽  
Tomas G. Villa ◽  
Herman J. Phaff
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Polypeptide Chain ◽  
Activation Energies ◽  
Partial Characterization ◽  
Effect Of Ph ◽  
Single Polypeptide Chain ◽  
Exclusion Chromatography ◽  
Single Polypeptide

The intracellular–periplasmic exo-1,3-β-glucanase (EC 3.2.1.58) has been extracted from the yeast Kluyveromyces aestuarii and purified to immunoelectrophoretic homogeneity by ion-exchange and gel-exclusion chromatography. The kinetic constants and activation energies for laminarin, p-nitrophenyl-β-D-glucoside, and pustulan have been determined, along with the effect of pH. Evidence is presented indicating that the enzyme is composed of a single polypeptide chain, about 24% carbohydrates, and its molecular weight was estimated to be 43 000.

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.

scholarly journals Characterization of human thyroxine-binding globulin. Evidence for a single polypeptide chain

1977 ◽  
Vol 252 (23) ◽  
pp. 8713-8718 ◽  
Author(s):  
M.C. Gershengorn ◽  
S.Y. Cheng ◽  
R.E. Lippoldt ◽  
R.S. Lord ◽  
J. Robbins
Keyword(s):  
Polypeptide Chain ◽  
Thyroxine Binding Globulin ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

Synthesis of very high molecular weight thyroglobulin in three heterologous systems

1980 ◽  
Vol 58 (5) ◽  
pp. 446-455 ◽  
Author(s):  
Margaret C. Eggo ◽  
Gerard N. Burrow
Keyword(s):  
Molecular Weight ◽  
Protease Inhibitors ◽  
Wheat Germ ◽  
Polypeptide Chain ◽  
Degradation Products ◽  
Xenopus Laevis Oocytes ◽  
Single Polypeptide Chain ◽  
Reticulocyte Lysate ◽  
Single Polypeptide ◽  
Very High

Calf thyroid RNA has been translated in the wheat germ and messenger-dependent reticulocyte lysate cell free systems and in Xenopus laevis oocytes. Peptides immunologically related to and comigrating with 330 000 molecular weight thyroglobulin as well as both larger and smaller immunopeptides have been synthesized. The smaller molecular weight peptides were due at least in part to degradation during incubation despite the presence of protease inhibitors. The larger molecular weight peptides could represent degradation products of a single polypeptide chain with a molecular weight of 660 000. The 330 000 molecular weight peptides would then represent cleavage of the protomer into two subunits. To support this possibility, thyroid polysomal RNA large enough to code for a peptide with a molecular weight of 660 000 has been shown to be active in thyroglobulin synthesis and to maintain its integrity under denaturing conditions.

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.

Debranching enzyme from rabbit skeletal muscle; Evidence for the location of two active centres on a single polypeptide chain

FEBS Letters ◽  
1975 ◽  
Vol 58 (1-2) ◽  
pp. 181-185 ◽  
Author(s):  
Edna J. Bates ◽  
Gillian M. Heaton ◽  
Carol Taylor ◽  
John C. Kernohan ◽  
Philip Cohen
Keyword(s):  
Skeletal Muscle ◽  
Polypeptide Chain ◽  
Rabbit Skeletal Muscle ◽  
Debranching Enzyme ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Active Centres
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