Results 1 to 10 of about 149 (147)
On the evolution of beta-galactosidase. [PDF]
The amino acid sequence of beta-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1.23) has been compared to itself and to other proteins. Two segments, each of about 380 amino acids, comprising the first three-fourths of the polypeptide chain, were found to be very similar to each other. It is concluded that they are homologous.
I Zabin, J M Hood, A V Fowler
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beta-Galactosidase chimeras: primary structure of a lac repressor-beta-galactosidase protein. [PDF]
A protein possessing both lac repressor and beta-galactosidase activities in a single polypeptide of about 155,000 daltons was purified from a deletion mutant of Escherichia coli in which the lacI and Z genes are fused. A 77-residue cyanogen bromide peptide containing the fusion joint was isolated.
Jürgen Kania+4 more
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Senescence‐associated β‐galactosidase is lysosomal β‐galactosidase [PDF]
SummaryReplicative senescence limits the proliferation of somatic cells passaged in culture and may reflect cellular aging in vivo. The most widely used biomarker for senescent and aging cells is senescence‐associated β‐galactosidase (SA‐β‐gal), which is defined as β‐galactosidase activity detectable at pH 6.0 in senescent cells, but the origin of SA‐β‐
Bo Yun Lee+9 more
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A novel Arthrobacter beta-galactosidase with homology to eucaryotic beta-galactosidases
An Arthrobacter beta-galactosidase has homology with the lysosomal acid beta-galactosidases from humans and mice and with a Xanthomonas manihotis enzyme. Phylogenetic analysis of the deduced amino acid sequence showed an unusual pattern, with this procaryotic enzyme clustering within the animal clade.
K Wang+2 more
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Beta galactosidases in Arabidopsis and tomato–a mini review [PDF]
Beta galactosidases (BGALs) are glycosyl hydrolases that remove terminal β-D-galactosyl residues from β-D-galactosides. There are 17 predicted BGAL genes in the genomes of both Arabidopsis (BGAL1–17) and tomato (TBG1–17). All tested BGALs have BGAL activity but their distinct expression profiles and ancient phylogenetic separation indicates that these ...
Balakumaran Chandrasekar+3 more
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Inhibitory activity of pyridindolol on .BETA.-galactosidase.
The activity of pyridindolol in inhibiting beta-galactosidases obtained from various sources has been studied. Whereas acid bovine liver beta-galactosidase (optimal pH 4.0) was not affected by this compound, neutral bovine liver beta-galactosidase (pH-optimum = 7.0) was inhibited by pyridindolol in reaction mixtures of pH 4.0 approximately 5.0.
Michihiko Kumagai+2 more
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Structure of pyridindolol, inhibitor of .BETA.-galactosidase.
Pyridindolol is a product of a streptomyces and exhibits inhibitory activity against bovine liver beta-galactosidase. The structure of pyridindilol, 1-[1(R), 2-dihydroxyethyl]-3-hydroxymethyl-9H-pyrido[3,4-b] indole, has been established by spectroscopic analyses and an X-ray structure determination.
Hamao Umezawa+5 more
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Small intestinal beta-galactosidase activity in the horse [PDF]
Two enzymes having lactase activity are present in the equine small intestine. The first, the digestive enzyme, neutral beta-galactosidase, declines in activity from birth to three years, disappearing completely between 3 and 4 years of age. The other, the soluble lysosomal enzyme, acid beta-galactosidase, having affinity for lactose and a synthetic ...
F. W. G. Hill+2 more
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Structure of a beta-galactosidase gene of Bacillus stearothermophilus [PDF]
The nucleotide sequence of the bgaB gene, which encodes the thermostable beta-galactosidase I of Bacillus stearothermophilus, and its flanking region was determined. A 2,016-base-pair open reading frame observed was concluded to be for beta-galactosidase I (Mr 78,051) from observations that the amino acid composition of the enzyme and the sequence of ...
S Negoro+3 more
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Mechanism of the rel defect in beta-galactosidase synthesis [PDF]
Relaxed (relA) mutants of Escherichia coli are defective in beta-galactosidase synthesis during amino acid limitation. We show here that this defect comprises both a transcriptional component and a translational component.
J Gallant, P Dennis, D Foley
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