Processing and activation of recombinant mouse mastocytoma histidine decarboxylase in the particulate fraction of Sf9 cells by porcine pancreatic elastase

S Tanaka; T Fukui; J Yamamoto; Y Shima; T Kume; M Ohgo; A Ichikawa

doi:10.1016/0167-4838(95)00185-w

Processing and activation of recombinant mouse mastocytoma histidine decarboxylase in the particulate fraction of Sf9 cells by porcine pancreatic elastase

Biochim Biophys Acta. 1995 Nov 15;1253(1):9-12. doi: 10.1016/0167-4838(95)00185-w.

Authors

S Tanaka¹, T Fukui, J Yamamoto, Y Shima, T Kume, M Ohgo, A Ichikawa

Affiliation

¹ Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.

PMID: 7492605
DOI: 10.1016/0167-4838(95)00185-w

Abstract

Mature 53 kDa histidine decarboxylase (HDC) peptide is produced from a precursor 74 kDa peptide. The mechanism of specific cleavage by processing enzyme is unknown. Using the recombinant mouse 74 kDa HDC, we found that porcine pancreatic elastase specifically converted the inactive 74 kDa HDC to its active form of 53 kDa HDC.

MeSH terms

Animals
Cell Line
Chromatography, Agarose
Endopeptidases / metabolism
Histidine Decarboxylase / chemistry
Histidine Decarboxylase / isolation & purification
Histidine Decarboxylase / metabolism*
Immunoblotting
Mast-Cell Sarcoma / enzymology
Mice
Molecular Weight
Pancreas / enzymology
Pancreatic Elastase / metabolism*
Protein Processing, Post-Translational*
Recombinant Fusion Proteins / chemistry
Recombinant Fusion Proteins / isolation & purification
Recombinant Fusion Proteins / metabolism
Solubility
Swine

Substances

Recombinant Fusion Proteins
Endopeptidases
Pancreatic Elastase
Histidine Decarboxylase