HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Holmes, W. E. Articles by Collen, D. Search for Related Content PubMed PubMed Citation Articles by Holmes, W. E. Articles by Collen, D. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 262, Issue 4, 1659-1664, 02, 1987

Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin)

WE Holmes, L Nelles, HR Lijnen and D Collen

The plasma protein alpha 2-antiplasmin is the main physiological inhibitor of the serine protease plasmin, which is responsible for the dissolution of fibrin clots. We have determined the primary structure of mature human alpha 2-antiplasmin by DNA sequencing of overlapping cDNA fragments prepared from human liver mRNA. cDNA clones were identified by hybridization with a 48-base pair deoxyoligonucleotide probe deduced from the sequence of a 16-amino acid peptide of alpha 2- antiplasmin. Mature human alpha 2-antiplasmin contains 452 amino acids. It is homologous (23-28%) with five other proteins belonging to the serine protease inhibitor (serpin) superfamily. Its reactive site, i.e. the peptide bond cleaved by reaction with its primary target enzyme, plasmin, consists of Arg364-Met365. This dipeptide corresponds to the reactive site Met358-Ser359 of the archetypal serpin, alpha 1- antitrypsin.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				V. J. Christiansen, K. W. Jackson, K. N. Lee, and P. A. McKee The effect of a single nucleotide polymorphism on human {alpha}2-antiplasmin activity Blood, June 15, 2007; 109(12): 5286 - 5292. [Abstract] [Full Text] [PDF]

				N. A. Booth and L. Thomas A snip enhances {alpha}2-antiplasmin Blood, May 15, 2004; 103(10): 3612 - 3612. [Full Text] [PDF]

				H.R. Lijnen, K. Okada, O. Matsuo, D. Collen, and M. Dewerchin alpha 2-Antiplasmin Gene Deficiency in Mice Is Associated With Enhanced Fibrinolytic Potential Without Overt Bleeding Blood, April 1, 1999; 93(7): 2274 - 2281. [Abstract] [Full Text] [PDF]

				J Potempa, B. Shieh, and J Travis Alpha-2-antiplasmin: a serpin with two separate but overlapping reactive sites Science, August 5, 1988; 241(4866): 699 - 700. [Abstract] [PDF]

				W. Holmes, H. Lijnen, L Nelles, C Kluft, H. Nieuwenhuis, D. Rijken, and D Collen Alpha 2-antiplasmin Enschede: alanine insertion and abolition of plasmin inhibitory activity Science, October 9, 1987; 238(4824): 209 - 211. [Abstract] [PDF]

				A. Zhou, R. W. Carrell, and J. A. Huntington The Serpin Inhibitory Mechanism Is Critically Dependent on the Length of the Reactive Center Loop J. Biol. Chem., July 13, 2001; 276(29): 27541 - 27547. [Abstract] [Full Text] [PDF]

				J. A. Irving, R. N. Pike, A. M. Lesk, and J. C. Whisstock Phylogeny of the Serpin Superfamily: Implications of Patterns of Amino Acid Conservation for Structure and Function Genome Res., December 1, 2000; 10(12): 1845 - 1864. [Abstract] [Full Text]