title: Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis.
abstract: We report that fragments of amino acid sequence recently described for tripeptidyl-peptidase I (TPP I) show that it is the rat homologue of the human CLN2 gene product that is deficient in classical late-infantile neuronal ceroid lipofuscinosis. This is unexpected, since the CLN2 protein has been thought to be a carboxyl-dependent endopeptidase, but TPP I is an exopeptidase possibly of serine-type.
authors.affiliation: MRC Molecular Enzymology Laboratory, Babraham Institute, Cambridgeshire, UK.
authors.forename: N D
authors.initials: ND
authors.lastname: Rawlings
authors.forename: A J
authors.initials: AJ
authors.lastname: Barrett
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D010450:Endopeptidases / Q000032:analysis*; D006801:Humans; D008969:Molecular Sequence Data; D009472:Neuronal Ceroid-Lipofuscinoses / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases / Q000032:analysis*; D016415:Sequence Alignment; D057057:Serine Proteases; D000091346:Tripeptidyl-Peptidase 1