PMID: 9003440Jan 4, 1997Paper

Purification and characterization of hepsin from rat liver microsomes

Biochimica Et Biophysica Acta
A ZhukovM Ingelman-Sundberg

Abstract

Hepsin, a putative cell-surface serine proteinase, has been isolated from the microsomal membranes of rat liver and purified to homogeneity by hydroxyapatite, DEAE-Sepharose, and benzamidine-Sepharose chromatography. The course of purification was monitored using antibodies raised against a 20-mer peptide at the C-terminus of rat hepsin, and the identity of the purified protein was confirmed by partial amino-acid sequencing. A single-chain precursor of ca. 50 kDa found in the microsomes underwent spontaneous maturation in the course of purification so that the last, affinity chromatography, step recovered only the mature form which dissociated to subunits of 31 and 19 kDa under reducing SDS-PAGE. Proteinase digestion experiments with microsomal vesicles are consistent with the luminal orientation of the precursor C-terminus, which would result in its extracellular orientation upon transportation to the cell surface. [3H]diisopropylfluorophosphate covalently binds to the large subunit showing it to be the catalytic one. The N-terminal sequencing of this subunit demonstrates that the zymogen is converted to the active serine proteinase by cleavage at the Arg161-Ile162 site. Activity measurements with short synthetic peptides show...Continue Reading

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Citations

Aug 30, 2008·International Journal of Cancer. Journal International Du Cancer·Jiangyong MiaoSandra Orsulic
Apr 23, 2010·Biological & Pharmaceutical Bulletin·Shinji NakamaYoko Aniya
May 29, 2010·The Biochemical Journal·Toni M AntalisSarah Netzel-Arnett
Aug 10, 2019·The Biochemical Journal·Lina WangQingyu Wu
Dec 11, 2020·The FEBS Journal·Shuo LiQingyu Wu
Feb 23, 2020·Biochimica Et Biophysica Acta. General Subjects·Cristina ZivkoPaola Luciani
Dec 21, 2018·Journal of Medicinal Chemistry·Vishnu C DamalankaJames W Janetka

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