Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 38, Issue 3-5, Pages 255-258Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2006.03.001
Keywords
non-mulberry silkworm; peduncle sericin; SDS-PAGE; CID spectroscopy
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A high molecular weight water-soluble glue protein, sericin was identified in the cocoon peduncle (a strong thread connecting the cocoons to the branches of the tree with a ring) of the tropical tasar silkworm, Antheraea mylitta. The sericin was isolated by 8 M urea containing 1% sodium dodecyl sulfate and beta-mercaptoethenol (2%) or by 1% sodium chloride. The protein was purified by gel filtration chromatography. In SDS-PAGE, a single band of approximately 200 kDa was detected both in non-reducing and reducing conditions. Amino acid analysis showed that the protein is enriched in glycine and serine. There is a slight difference observed in amino acid composition between the sericin from cocoon peduncle and cocoon of A. mylitta. Secondary structure estimation by circular dichroism spectrometry showed 36.7% beta-sheets, 52.7% random coils, 10.6% turns and no helices. (c) 2006 Elsevier B.V. All rights reserved.
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