Molecular weight of the undegraded polypeptide chain of Pseudomonas amyloderamosa isoamylase

1980 ◽  
Vol 611 (2) ◽  
pp. 390-393 ◽  
Author(s):  
Akinori Amemura ◽  
Yoshio Konishi ◽  
Tokuya Harada
Keyword(s):  
Molecular Weight ◽  
Polypeptide Chain

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 On the Molecular Weight of Polypeptide Chain of Sweet Potao β-Amylase

1971 ◽  
Vol 35 (5) ◽  
pp. 778-780 ◽  
Author(s):  
Yasuhito TAKEDA ◽  
Susumu HIZUKURI ◽  
Takeshi MURAKAMI
Keyword(s):  
Molecular Weight ◽  
Polypeptide Chain

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.

Weitere Untersuchungen zur Aminosäuresequenz des Melittins

1969 ◽  
Vol 24 (1) ◽  
pp. 33-35 ◽  
Author(s):  
Joachim Jentsch
Keyword(s):  
Aqueous Solution ◽  
Molecular Weight ◽  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Optical Rotatory Dispersion ◽  
Optical Rotatory ◽  
Surface Active ◽  
Α Helix

Melittin is the (main) toxic peptide of bee venom having a molecular weight of 2840, with a known sequence (s. fig. 1). Optical rotatory dispersion of non-crystalline melittin in aqueous solution suggests that the polypeptide chain is random, although 7% α-helix has been determined. These results are in agreement with the amino acid sequence of melittin and the assumption that the biological activity is attributable to its surface active character.

scholarly journals Molecular weight and amino acid composition of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R61

1973 ◽  
Vol 135 (3) ◽  
pp. 463-468 ◽  
Author(s):  
J.-M. Frère ◽  
J.-M. Ghuysen ◽  
H. R. Perkins ◽  
M. Nieto
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polypeptide Chain

A procedure allowing the purification of milligram amounts of the exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R61 to protein homogeneity (95% purity) is described. The isolated protein has a molecular weight of about 38000 and consists of one polypeptide chain. Its amino acid composition is presented.

scholarly journals Plasmic degradation of crosslinked fibrin. I. Structural analysis of the particulate clot and identification of new macromolecular-soluble complexes

Blood ◽  
1980 ◽  
Vol 56 (3) ◽  
pp. 456-464 ◽  
Author(s):  
CW Francis ◽  
VJ Marder ◽  
SE Martin
Keyword(s):  
Molecular Weight ◽  
Structural Analysis ◽  
High Molecular Weight ◽  
Polypeptide Chain ◽  
Degradation Products ◽  
Fibrin Clot ◽  
Proteolytic Cleavages ◽  
Soluble Complexes ◽  
Covalently Bound

Abstract Plasmic degradation of crosslinked fibrin has been studied to identify the proteolytic cleavages that convert the clot into a soluble lysate and also to identify the derivatives that are likely to circulate during clot dissolution. Initial polypeptide chain cleavages do not disrupt the solid clot matrix. With continued exposure to plasmin, high molecular weight derivatives are produced that remain attached to the clot by noncovalent forces. Further degradation then results in the liberation into solution of several large, noncovalently bound complexes. Progressive degradation of the largest, initially liberated complexes to the terminal derivatives, DD/E, DD, and E, occurs in solution after their release from the clot. As the fibrin clot is exposed to plasmin for longer intervals, progressive dissolution occurs, but the structure of the covalently bound insoluble fibrin core, the noncovalently attached derivatives, and the liberated complexes remains constant. Since much of the initially liberated protein is in complexes larger than DD/E, these derivatives probably represent the more prevalent plasmic degradation products of crosslinked fibrin in vivo.

A MvaI PCR-RFLP detecting a silent allele at the goat α-lactalbumin locus

2003 ◽  
Vol 70 (3) ◽  
pp. 355-357 ◽  
Author(s):  
Gianfranco Cosenza ◽  
Daniela Gallo ◽  
Rosa Illario ◽  
Paola di Gregorio ◽  
Carmela Senese ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Common Ancestor ◽  
Polypeptide Chain ◽  
Serum Proteins ◽  
Transcription Unit ◽  
Human Lysozyme ◽  
Similar Molecular Weight ◽  
Pcr Rflp ◽  
Lactose Synthase ◽  
Silent Allele

Alpha-lactalbumin (α-la), a calcium metalloprotein, is one of the major serum-proteins in ruminant milk (Jenness, 1982) and induces lactose synthesis in the mammary gland by interacting with the enzyme UDP-galactosyltransferase, giving rise to the heterodimer enzyme lactose synthase (Ebner & Brodbeck, 1968; Kuhn, 1983). The goat α-la transcription unit (LALBA), located on chromosome 5 (Hayes et al. 1993), is organized in 4 exons varying in length from 75 nucleotides (3rd exon) to 329 nucleotides (4th exon) coding for a 123-amino acid polypeptide chain (Vilotte et al. 1991). According to the strong similarity between bovine α-la (Vilotte et al. 1987) and human lysozyme (similar molecular weight, the same number of S-S bonds, identical N and C terminal residues; Peters et al. 1989), it has been proposed that both genes arose from a common ancestor (Vilotte et al. 1991).

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