title: Characterization of the immunoglobulin A protease of Ureaplasma urealyticum.
abstract: Ureaplasma urealyticum strains of all serotypes express a specific human immunoglobulin A1 protease that cleaves immunoglobulin A1 to produce intact Fab and Fc fragments. The use of a variety of inhibitors suggests that the enzyme is a serine protease. N-terminal sequencing of the Fc digestion product showed that the enzyme cleaves between the proline and threonine residues 235 and 236 in the hinge region of the heavy chain of immunoglobulin A1.
authors.affiliation: Department of Biochemistry and Microbiology, University of St. Andrews, Fife, Scotland.
authors.forename: R K
authors.initials: RK
authors.lastname: Spooner
authors.forename: W C
authors.initials: WC
authors.lastname: Russell
authors.forename: D
authors.initials: D
authors.lastname: Thirkell
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D007071:Immunoglobulin A, Secretory / Q000378:metabolism; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011480:Protease Inhibitors / Q000494:pharmacology; D012697:Serine Endopeptidases; D016990:Ureaplasma urealyticum / Q000201:enzymology*
chemical_list: D007071:Immunoglobulin A, Secretory; D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase