Porcine Submaxillary Mucin Forms Disulfide-bonded Dimers between Its Carboxyl-terminal Domains
Open Access
- 1 April 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (16) , 9845-9850
- https://doi.org/10.1074/jbc.271.16.9845
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Site-directed mutagenesis of virtually any plasmid by eliminating a unique siteAnalytical Biochemistry, 1992
- Assembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acids.The Journal of cell biology, 1991
- Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferaseAnalytical Biochemistry, 1991
- Cloning and cDNA sequence of a bovine submaxillary gland mucin-like protein containing two distinct domains.Proceedings of the National Academy of Sciences, 1990
- An integumentary mucin (FIM-B.1) from Xenopus laevis homologous with the von Willebrand factorBiochemistry, 1990
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988
- Identification of disulfide-bridged substructures within human von Willebrand factorBiochemistry, 1987
- A human beta-actin expression vector system directs high-level accumulation of antisense transcripts.Proceedings of the National Academy of Sciences, 1987
- pEMBL: a new family of single stranded plasmidsNucleic Acids Research, 1983
- N-hydroxysulfosuccinimide active esters: bis(N-hydroxysulfosuccinimide) esters of two dicarboxylic acids are hydrophilic, membrane-impermeant, protein cross-linkersBiochemistry, 1982