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Isolation of ovocleidin-116 from chicken eggshells, correction of its amino acid sequence and identification of disulfide bonds and glycosylated Asn

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Mann,  K.
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Mann, K., Hincke, M. T., & Nys, Y. (2002). Isolation of ovocleidin-116 from chicken eggshells, correction of its amino acid sequence and identification of disulfide bonds and glycosylated Asn. Matrix Biology, 21(5), 383-387.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6EA0-6
Abstract
Fractionation of the soluble chicken eggshell matrix by chromatographic methods yielded 13 endogenous proteolytic fragments of the eggshell-specific proteoglycan core protein ovocleidin-116. The N-terminal amino acid sequences of these fragments in general confirmed the recently cDNA-deduced sequence of ovocleidin-116, with one exception. One fragment yielded a completely new sequence and was instrumental in detecting a frame shift error in the nucleotide sequence. The correction yielded a new sequence which was 38 amino acids shorter than before and contained a 57-amino acid long novel C- terminal sequence.(1) The predicted sequence of ovocleidin-116 contained two consensus N-glycosylation sites, only one of which (Asn62) was found to be fully modified. A disulfide bond was identified between Cys31 and 42 implying that Cys329 and 421 form a second disulfide bond. Finally, the yield of fragments indicated that ovocleidin-116 is a major component of the chicken eggshell matrix. (C) 2002 Elsevier Science B.V. and International Society of Matrix Biology. All rights reserved.