The amino acid sequence in a fraction of the fibroin of <i>Bombyx mori</i>

Lucas, François; Shaw, J. T. B.; Smith, S. G.

doi:10.1042/bj0660468

Cited by 116 publications

(32 citation statements)

References 14 publications

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“…5 Thus we had to use ␣-chymotrypsin because the ␣-chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds at the carboxyl groups of tyrosine, and is very useful for hydrolyzing silk fibroins containing about 5% tyrosine by weight. 6 Furthermore, it was previously reported that the acylation of protein can be performed completely with the use of ␣-chymotrypsin. 7 The resulting monomer was confirmed by the change of solubility in the good solvent for SFP and that of UV-visible spectra of SFP before and after acylation.…”

Section: Preparation Of Sfp Monomermentioning

confidence: 99%

Synthesis and characterization of spinning poly(acrylonitrile‐co‐silk fibroin peptide)s

Chen

Suzuki

Kimura

et al. 2004

J of Applied Polymer Sci

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A novel spinning acrylic polymer containing silk protein was synthesized by copolymerization of acrylonitrile (AN) and silk fibroin peptide (SFP) modified by acryloyl chloride (AC) with vinyl groups. From results of the examination to the chemical compositions, we established that the modified SFP is more reactive than AN in the copolymerization. The intrinsic viscosity values of these copolymers showed that the copolymers have good spinnability, which were synthesized under the condition of adding a trace of metal ions into the synthesizing solvent. These copolymers exhibited good thermal property. The fiber based on the poly(acrylonitrile-co-silk fibroin peptide) was prepared and characterized by SEM, FTIR measurement of its shell and core flakes, and moisture absorption. The fiber exhibited a smooth surface and could be assumed to have excellent adhesive property between SFP and PAN. Furthermore, these fibers showed a core-shell structure and excellent moisture absorption.

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Section: Preparation Of Sfp Monomermentioning

confidence: 99%

Synthesis and characterization of spinning poly(acrylonitrile‐co‐silk fibroin peptide)s

Chen

Suzuki

Kimura

et al. 2004

J of Applied Polymer Sci

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“…A closer examination shows that over 20°/, of the sequence takes the form of two runs of (Gly-X),. This arrangement is reminiscent of the structure of Bombyx mori silk fibroin [20].…”

Section: Trp-pro-phementioning

confidence: 99%

The Primary Structure of a Protein, Component 0.62, Rich in Glycine and Aromatic Residues, Obtained from Wool Keratin

Dopheide¹

1973

European Journal of Biochemistry

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The amino acid sequence of component 0.62, a protein derived from wool keratin, with molecular weight of 6950, rich in glycine and aromatic residues, has been determined. The prot,ein contains no lysine, histidine, glutamic acid, isoieucine or methionine. Of the total residues, more than 5001, are glycine and aromatic amino acids. The sequence contains two sections rich in glycine, (Gly-X), and (Gly-X),, which comprise 22O/, of the sequence.The a-keratins, as exemplified by wool, hoof, horn and animal hairs and quills, consist of filamentous units, the microfibrils, embedded in a nonfilamentous matrix. The filaments have been identified with a set of highly a-helical proteins, containing it lower percentage of sulphur than the parent material, while the non-filamentous matrix between the microfibrils consists largely of a group of heterogeneous proteins, containing a higher percentage of sulphur than the parent material (for an up-to-date summary of the present position see [l]). Both of these types of protein have been investigated. A considerable amount is known about the primary structure of certain of their components [2--41.A third group of proteins, probably derived from the matrix, with an as-yet undefined function and structure is also present. This class is extremely rich in glycine and aromatic residues [5] which together may account for more than one half of the total amino acid residues in these proteins. These proteins are hereafter referred to as "tyrosine-rich proteins".This work describes the detailed study of the sequence of one of these tyrosine-rich components of wool obtained in a soluble form by the reduction of the disulphide bonds of wool and stabilization of the thiols by alkylation with iodoacetic acid MATERIALS AND METHODSThe tyrosine-rich protein, a gift from Dr J. M. Gillespie, was prepared from fine, non-peppin Merino wool as described in the accompanying paper Enzymic DigestionEnzymic digestion of the protein was performed at l o / , protein concentration with a 1/100 (w/w) ratio of enzyme to substrate. The buffer used for tryptic, chymotryptic and thermolytic digestions was N-ethylmorpholine acetate (0.1 M, pH 8.0). Carboxypeptidase hydrolysis of peptides was generally done on 0.05 pmol peptide in 100 pl 0.1 M NH,-HCO, with I0 pg carboxypeptidase A for various times a t 25 "C. Progress of the reaction was monitored by paper electrophoresis a t pH 1.9 or by amino acid analysis. Peptide PurificationAfter gel chromatography, peptides were further purified by high-voltage paper electrophoresis a t pH 1.9 or pH 3.5. Whatman paper 3 MM was used throughout a t 50 V/cm. The electrophoretic mobility a t pH 6.5 relative to aspartic acid ( ? A s p = -1.0 a t pH 6.5) [8] was the criterion used to determine the state of the single aspartic acid found in the protein.Paper chromatography in butanol-acetic acidwater-pyridine (15 : 3 : 12 : 10, v/v/v/v) was also used occasionally to separate peptide mixtures.

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“…In the early 1950s, Lucas et al 7 used acid hydrolysis followed by ion-exchange chromatography to separate and identify the amino acids. These workers characterized the amino acid composition of both sericin and fibroin of Bombyx mori and Antheraea silks.…”

Section: Introductionmentioning

confidence: 99%

Studies on Indian silk. I. Macrocharacterization and analysis of amino acid composition

Sen

K²

2004

J of Applied Polymer Sci

126

110

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This first in a series of articles characterized the different varieties of Indian silk for their macrostructural parameters, such as filament length, degumming loss, denier, cross section, moisture regain, and intrinsic viscosity, for example. The results of amino acid analysis using a reverse-phase technique were also reported. Five Indian silk varieties-two mulberry (bivoltine and crossbreed) and three nonmulberry (tasar, muga, and eri)-were investigated. The differences existing between the different varieties and the extent of lengthwise variations within a cocoon in the dimensional and macrostructural parameters were discussed. It was observed that denier of the filament decreases considerably from the outer to the inner layers, whereas density showed an increasing trend in all the varieties. Both the mulberry silks demonstrated lower moisture regain. Electron micrographs of all the nonmulberry varieties showed microvoids in their cross section. Fraction studies showed the development of mushroom structure on the tips. In both types of mulberry silk, glycine, alanine, and serine constitute about 82% of the amino acids present. On the other hand, in nonmulberry silks, these constitute about 73% with a high proportion of alanine. The nonmulberry varieties showed a substantial proportion of amino acids with bulky side groups. Similarly, the higher hydrophilic to hydrophobic amino acid ratio (9.06 -9.85) for nonmulberry silks, compared against that of the mulberry varieties (5.29 -6.22), was shown to be responsible for the higher moisture content of nonmulberry silks. Cystine and methionine were present in all the varieties. The higher intrinsic viscosity of nonmulberry varieties suggested their higher molecular weight. Through amino acid analysis, it was shown that there is no difference in chemical architecture between the outer and the inner layers of cocoons.

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The amino acid sequence in a fraction of the fibroin of Bombyx mori

Cited by 116 publications

References 14 publications

Synthesis and characterization of spinning poly(acrylonitrile‐co‐silk fibroin peptide)s

Synthesis and characterization of spinning poly(acrylonitrile‐co‐silk fibroin peptide)s

The Primary Structure of a Protein, Component 0.62, Rich in Glycine and Aromatic Residues, Obtained from Wool Keratin

Studies on Indian silk. I. Macrocharacterization and analysis of amino acid composition

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