Possible involvement of cathepsin L in processing of rat liver hexokinase to eliminate mitochondria-binding ability

Hiroshi Okazaki, Chiemi Tanl, Miyuki Ando, Kyoko Ishii, Sadahiko Ishibashi, Yukio Nishimura, Keitaro Kato

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Abstract

A previously found proteinase possibly involved in the modification of hexokinase to eliminate the mitochondria-binding ability without appreciable change in the catalytic activity (called hexokinase-processing enzyme hereafter), was purified by sequential chromatographies from rat liver and its properties were examined. The hexokinase-processing enzyme had carbohydrate moieties as evidenced by adsorption on immobilized concanavalin A, and had a molecular weight of about 23,000 as estimated by SDS-PAGE and gel filtration chromatography. Benzyloxycarbonyl-phenylalanyl-L-arginlne-4-methylcou- maryl-7-amlde (Z-Phe-Arg-MCA)-hydrolyzing activity was co-purified with this processing activity throughout the purification, while the hydrolyzing activity for benzyloxycar bonyl-L-arglnyl-L-arglnine-4-methylcoumaryl-7-amlde (Z-Arg-Arg-MCA) was not. The processing activity, as well as Z-Phe-Arg-MCA hydrolyzing activity, was highly sensitive to cysteine proteinase inhibition, for example, by leupeptin and N[N-3-(trans-carbox-irane-2-carbonyl)-L-leucyl] agmatine (E-64). Furthermore, the enzyme preparation reacted with an antibody against cathepsin L purified from rat kidney. These results indicated that cathep sin L may be involved In the above-mentioned processing of hexokinase.

Original languageEnglish
Pages (from-to)409-413
Number of pages5
JournalJournal of biochemistry
Volume112
Issue number3
DOIs
Publication statusPublished - Jan 1 1992

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Cathepsin L
Mitochondria
Hexokinase
Liver
Rats
Processing
Chromatography
Enzymes
Agmatine
Cysteine Proteases
Concanavalin A
Adsorption
Gel Chromatography
Polyacrylamide Gel Electrophoresis
Peptide Hydrolases
Molecular Weight
Carbohydrates
Purification
Catalyst activity
Kidney

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Possible involvement of cathepsin L in processing of rat liver hexokinase to eliminate mitochondria-binding ability. / Okazaki, Hiroshi; Tanl, Chiemi; Ando, Miyuki; Ishii, Kyoko; Ishibashi, Sadahiko; Nishimura, Yukio; Kato, Keitaro.

In: Journal of biochemistry, Vol. 112, No. 3, 01.01.1992, p. 409-413.

Research output: Contribution to journalArticle

Okazaki, Hiroshi ; Tanl, Chiemi ; Ando, Miyuki ; Ishii, Kyoko ; Ishibashi, Sadahiko ; Nishimura, Yukio ; Kato, Keitaro. / Possible involvement of cathepsin L in processing of rat liver hexokinase to eliminate mitochondria-binding ability. In: Journal of biochemistry. 1992 ; Vol. 112, No. 3. pp. 409-413.
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