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Titolo:
Immunological detection of alkaline-diaminobenzidine-negativeperoxisomes of the nematode Caenorhabditis elegans - Purification and unique pH optima of peroxisomal catalase
Autore:
Togo, SH; Maebuchi, M; Yokota, S; Bun-ya, M; Kawahara, A; Kamiryo, T;
Indirizzi:
Hiroshima Univ, Fac Integrated Arts & Sci, Higashihiroshima 7398521, JapanHiroshima Univ Higashihiroshima Japan 7398521 hihiroshima 7398521, Japan Yamanashi Med Univ, Biol Lab, Tamaho, Yamanashi, Japan Yamanashi Med UnivTamaho Yamanashi Japan Lab, Tamaho, Yamanashi, Japan
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 5, volume: 267, anno: 2000,
pagine: 1307 - 1312
SICI:
0014-2956(200003)267:5<1307:IDOAO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
STEROL CARRIER PROTEIN-2; LIPID-TRANSFER PROTEIN; YEAST CANDIDA-TROPICALIS; ACYL-COENZYME-A; RAT-LIVER; THIOLASE; SEQUENCE; 3,3'-DIAMINOBENZIDINE; LOCALIZATION; MICROBODIES;
Keywords:
Caenorhabditis elegans; catalase; 3,3 '-diaminobenzidine; peroxidase; peroxisomes;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Kamiryo, T Hiroshima Univ, Fac Integrated Arts & Sci, Higashihiroshima 7398521, Japan Hiroshima Univ Higashihiroshima Japan 7398521 7398521, Japan
Citazione:
S.H. Togo et al., "Immunological detection of alkaline-diaminobenzidine-negativeperoxisomes of the nematode Caenorhabditis elegans - Purification and unique pH optima of peroxisomal catalase", EUR J BIOCH, 267(5), 2000, pp. 1307-1312

Abstract

We purified catalase-2 of the nematode Caenorhabditis elegans and identified peroxisomes in this organism. The peroxisomes of C. elegans were not detectable by cytochemical staining using 3,3'-diaminobenzidine, a commonly used method depending on the peroxidase activity of peroxisomal catalase at pH 9 in which genuine peroxidases are inactive. The cDNA sequences of C. elegans predict two catalases very similar to each other throughout the molecule, except for the short C-terminal sequence; catalase-2 (500 residues long) carries a peroxisomal targeting signal 1-like sequence (Ser-His-Ile), whereas catalase-1 does not. The catalase purified to near homogeneity from the homogenate of C. elegans cells consisted of a subunit of 57 kDa and was specifically recognized by anti-(catalase-2) serum but not by anti-(catalase-1) serum. Subcellular fractionation and indirect immunoelectron microscopyof the nematode detected catalase-2 inside vesicles judged to be peroxisomes using morphological criteria. The purified enzyme (220 kDa) was tetrameric, similar to many catalases from various sources, but exhibited unique pHoptima for catalase (pH 6) and peroxidase (pH 4) activities; the latter value is unusually low and explains why the peroxidase activity was undetectable using the standard alkaline diaminobenzidine-staining method. These results indicate that catalase-2 is peroxisomal and verify that it can be usedas a marker enzyme for C. elegans peroxisomes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 20:54:17