Purification and characterization of cathepsin J from rat liver

scientific article published in February 1992

Purification and characterization of cathepsin J from rat liver is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1111/J.1432-1033.1992.TB16647.X
P698PubMed publication ID1740150
P5875ResearchGate publication ID21415939

P2093author name stringN Katunuma
T Towatari
T Nikawa
P2860cites workMeasurement of protein using bicinchoninic acidQ26778491
Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins.Q30321506
Fluorimetric assays for cathepsin B and cathepsin H with methylcoumarylamide substratesQ42119374
The specific assay of arylsulphatase C, a rat liver microsomal marker enzymeQ42918414
The isolation of IgG from mammalian sera with the aid of caprylic acidQ47677816
P433issue1
P407language of work or nameEnglishQ1860
P1104number of pages13
P304page(s)381-393
P577publication date1992-02-01
P1433published inFEBS JournalQ1388041
P1476titlePurification and characterization of cathepsin J from rat liver
P478volume204

Reverse relations

cites work (P2860)
Q41855089Activation of procathepsin B in human hepatoma cells: the conversion into the mature enzyme relies on the action of cathepsin B itself
Q43022343Affinity Purification, Overexpression, and Characterization of Chaperonin 10 Homologues Synthesized with and without N-terminal Acetylation
Q48051247Cloning and characterization of the cDNA encoding mouse dipeptidyl peptidase I (cathepsin C).
Q34713891Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease
Q44078417Dipeptidyl peptidase I: importance of progranzyme activation sequences, other dipeptide sequences, and the N-terminal amino group of synthetic substrates for enzyme activity
Q64966672Distinct expression of mast cell tryptase and protease activated receptor-2 in synovia of rheumatoid arthritis and osteoarthritis.
Q38454446Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I).
Q71448128Interaction of human cathepsin C with chicken cystatin
Q72571002Lectin affinity chromatography
Q28295805Molecular cloning and sequence analysis of human preprocathepsin C
Q28176872New functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors
Q77376182Novel physiological functions of cathepsins B and L on antigen processing and osteoclastic bone resorption
Q24337142Oligomeric Structure and Substrate Induced Inhibition of Human Cathepsin C
Q70494348Participation of cathepsin B in processing of antigen presentation to MHC class II
Q36657045Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch.-Ham.
Q38845947Regulation of split anergy in natural killer cells by inhibition of cathepsins C and H and cystatin F.
Q24328833Simultaneous isolation of human kidney cathepsins B, H, L and C and their characterisation
Q28265084Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C
Q73077056Structure based development of novel specific inhibitors for cathepsin L and cathepsin S in vitro and in vivo
Q27635416Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain
Q72345450The mechanisms and regulation of procathepsin L secretion from osteoclasts in bone resorption

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