Coexistence of two kinds of 6-phospho-β-galactosidase in the cytosol of lactobacillus gasseri JCM1031

Masakatsu Suzuki; Tadao Saito; Takatoshi Itoh

doi:10.1271/bbb.60.708

Coexistence of two kinds of 6-phospho-β-galactosidase in the cytosol of lactobacillus gasseri JCM1031

Masakatsu Suzuki, Tadao Saito, Takatoshi Itoh

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

Lactobacillus (L.) gasseri JCM1031 has 2 kinds of 6-phospho-β-galactosidase (P-β-gal) in the cytosol. P-β-gal I was already isolated and characterized for our previous paper [Biosci. Biotech. Biochem., 60, 139–141 (1996)]. Another, P-ß-gal II, was purified to homogeneity through several liquid chromatographic steps for this paper. The molecular mass of the purified enzyme was estimated to be 58kDa by SDS–PAGE. The K_m and V_max for ONPGal-6P were 0.76 mM and 86.0 μmol/min/mg, respectively. Reducing reagents and Fe²⁺ ion activated the enzyme, but PCMB, Zn²⁺, and Hg²⁺ ions, and alkylation reagents strongly inhibited it. Twenty-five residues of the N-terminal amino acid sequence of the enzyme were identified. P-β-gal II was different from P-β-gal I in several characteristics.

Original language	English
Pages (from-to)	708-710
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	60
Issue number	4
DOIs	https://doi.org/10.1271/bbb.60.708
Publication status	Published - 1996 Jan

Keywords

6-phospho-β-galactosidase
Lactobacillus gasseri
Purification

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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title = "Coexistence of two kinds of 6-phospho-β-galactosidase in the cytosol of lactobacillus gasseri JCM1031",

abstract = "Lactobacillus (L.) gasseri JCM1031 has 2 kinds of 6-phospho-β-galactosidase (P-β-gal) in the cytosol. P-β-gal I was already isolated and characterized for our previous paper [Biosci. Biotech. Biochem., 60, 139–141 (1996)]. Another, P-{\ss}-gal II, was purified to homogeneity through several liquid chromatographic steps for this paper. The molecular mass of the purified enzyme was estimated to be 58kDa by SDS–PAGE. The Km and Vmax for ONPGal-6P were 0.76 mM and 86.0 μmol/min/mg, respectively. Reducing reagents and Fe2+ ion activated the enzyme, but PCMB, Zn2+, and Hg2+ ions, and alkylation reagents strongly inhibited it. Twenty-five residues of the N-terminal amino acid sequence of the enzyme were identified. P-β-gal II was different from P-β-gal I in several characteristics.",

keywords = "6-phospho-β-galactosidase, Lactobacillus gasseri, Purification",

author = "Masakatsu Suzuki and Tadao Saito and Takatoshi Itoh",

year = "1996",

month = jan,

doi = "10.1271/bbb.60.708",

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AU - Suzuki, Masakatsu

AU - Saito, Tadao

AU - Itoh, Takatoshi

PY - 1996/1

Y1 - 1996/1

N2 - Lactobacillus (L.) gasseri JCM1031 has 2 kinds of 6-phospho-β-galactosidase (P-β-gal) in the cytosol. P-β-gal I was already isolated and characterized for our previous paper [Biosci. Biotech. Biochem., 60, 139–141 (1996)]. Another, P-ß-gal II, was purified to homogeneity through several liquid chromatographic steps for this paper. The molecular mass of the purified enzyme was estimated to be 58kDa by SDS–PAGE. The Km and Vmax for ONPGal-6P were 0.76 mM and 86.0 μmol/min/mg, respectively. Reducing reagents and Fe2+ ion activated the enzyme, but PCMB, Zn2+, and Hg2+ ions, and alkylation reagents strongly inhibited it. Twenty-five residues of the N-terminal amino acid sequence of the enzyme were identified. P-β-gal II was different from P-β-gal I in several characteristics.

AB - Lactobacillus (L.) gasseri JCM1031 has 2 kinds of 6-phospho-β-galactosidase (P-β-gal) in the cytosol. P-β-gal I was already isolated and characterized for our previous paper [Biosci. Biotech. Biochem., 60, 139–141 (1996)]. Another, P-ß-gal II, was purified to homogeneity through several liquid chromatographic steps for this paper. The molecular mass of the purified enzyme was estimated to be 58kDa by SDS–PAGE. The Km and Vmax for ONPGal-6P were 0.76 mM and 86.0 μmol/min/mg, respectively. Reducing reagents and Fe2+ ion activated the enzyme, but PCMB, Zn2+, and Hg2+ ions, and alkylation reagents strongly inhibited it. Twenty-five residues of the N-terminal amino acid sequence of the enzyme were identified. P-β-gal II was different from P-β-gal I in several characteristics.

KW - 6-phospho-β-galactosidase

KW - Lactobacillus gasseri

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Coexistence of two kinds of 6-phospho-β-galactosidase in the cytosol of lactobacillus gasseri JCM1031

Abstract

Keywords

ASJC Scopus subject areas

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