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Titlebook: Glycoprotein Methods and Protocols; The Mucins Anthony P. Corfield Book 2000 Humana Press 2000

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发表于 2025-3-21 18:02:25 | 显示全部楼层 |阅读模式
书目名称Glycoprotein Methods and Protocols
副标题The Mucins
编辑Anthony P. Corfield
视频video
概述Includes supplementary material:
丛书名称Methods in Molecular Biology
图书封面Titlebook: Glycoprotein Methods and Protocols; The Mucins Anthony P. Corfield Book 2000 Humana Press 2000
描述The mucins (mucus glycoproteins) have long been a complex corner of glycoprotein biology. While dramatic advances in the separation, structural an- ysis, biosynthesis, and degradation have marked the progress in general glycop- tein understanding, the mucins have lagged behind. The reasons for this lack of progress have always been clear and are only now being resolved. The mucins are very large molecules; they are difficult to separate from other molecules present in mucosal secretions or membranes; they are often degraded owing to natural protective functions or to isolation methodology and their peptide and oligos- charide structures are varied and complex. Understanding these molecules has demanded progress in several major areas. Isolation techniques that protect the intact mucins and allow dissociation from other adsorbed but discrete molecules needed to be developed and accepted by all researchers in the field. Improved methods for the study of very large molecules with regard to their aggregation and polymerization were also needed. Structural analysis of the peptide domains and the multitude of oligosaccharide chains was required for smaller sample sizes, for multiple samp
出版日期Book 2000
版次1
doihttps://doi.org/10.1385/1592590489
isbn_softcover978-1-61737-149-3
isbn_ebook978-1-59259-048-3Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightHumana Press 2000
The information of publication is updating

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Separation and Identification of Mucins and Their Glycoformsse mucins share common features in that they are oligomeric in nature and consist of a variable number of monomers (subunits) linked in an end-to-end fashion via the agency of disulfide bonds. In addition, their polypeptides comprise regions of dense glycosylation interspersed with “naked” cysteine-rich domains (.–.).
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Identification of Glycosylation Sites in Mucin Peptides by Edman Degradationicroheterogeneity). Typically, the characterization of macro- and microheterogeneity has been dependent on the isolation of small peptides with only one glycosylation site. However, this is not possible with high molecular weight, heavily glycosylated domains such as those found in mucins.
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Mucin Domains to Explore Disulfide-Dependent Dimer Formationregion of tandem repeat sequences, flanked by cysteine-rich regions at each end, which are presumed to mediate polymerization. Secretory mucins contain approx 60–80% carbohydrate, with extensive .-glycosylation in the central tandem repeat regions, and N-linked oligosaccharides in the peripheral regions (.).
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Detection and Quantitation of Mucins Using Chemical, Lectin, and Antibody Methods starting point for development of a technique. Refer to Chapter 3 for detection of mucins in histological preparations (.); note, however, that many of the principles for selection of detection tools discussed herein are applicable to histological detection.
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