Rabbit liver alcohol dehydrogenase: Isolation and characterization of class I isozymes

Keung, Wing Ming; Yip, P.K.

doi:10.1016/s0006-291x(89)80068-3

Cited by 10 publications

(4 citation statements)

References 19 publications

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“…4). Consequently, the initial chromatographic patterns appear to confirm conclusions of two types of subunit with minor differences corresponding to isozyme arrangements for BC and CC [15]. However, total compositions failed to reveal any differences between BC and CC, showing that structural differences, if any, are minute.…”

Section: Tacacagacgccttccttggaagcagtcttcttctgattcctgtatcc~catcatctgtamentioning

confidence: 62%

“…Rabbit liver alcohol dehydrogenase class I was purified and separated into CC and BC forms as described [15]. In addition, small amounts of AC forms were obtained [15]. The enzyme forms were identified by starch-gel and urea-gel electrophoresis [21].…”

Section: Proteinsmentioning

confidence: 99%

“…In the present study, cDNA coding for rabbit liver class-I alcohol dehydrogenase was cloned and sequenced and two of the rabbit protein forms, corresponding to apparently homodimeric CC and heterodimeric BC [15] forms, were structurally analyzed at the peptide level. No evidence for microheterogeneities was obtained, neither by cDNA cloning, nor by peptide mapping and direct analysis.…”

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confidence: 99%

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Isozyme developments in mammalian class‐I alcohol dehydrogenase

Höög

Vagelopoulos

Yip

et al. 1993

European Journal of Biochemistry

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Isozyme patterns differ widely among the classical type (class I) of mammalian alcohol dehydrogenases. For the rabbit enzyme, the possibility of isozymes has been reported but structural evidence is lacking. This system was now studied at both the mRNA/cDNA and protein levels. Ten cDNA clones, coding for class‐I alcohol dehydrogenase, were isolated from a rabbit liver cDNA library using a human DNA fragment as probe. The cDNA spanned 1296 bp, including the entire coding region. All clones coded for the same polypeptide and Northern blots identified a single mRNA corresponding to about 1.5 kb. Comparison of two protein forms (CC and BC) by HPLC peptide fingerprinting and structural analysis revealed peptide segments identical in amino acid sequence. Consequently, direct protein analyses and Northern blots show the presence of only one primary translation product. The data suggest that lagomorphic alcohol dehydrogenase, like the rodent enzyme, is not as isozyme rich as it may appear superficially, and that secondary modifications contribute substantially to mammalian alcohol dehydrogenase multiplicity. The active center of the rabbit enzyme suggests similarities to the horse S, human γ, and rat enzyme structures, compatible with a steroid dehydrogenase activity shown experimentally. Typical class‐I properties were established by direct analysis and confirmed by structural properties (Km for cyclohexanol 0.8–1.1 mM, for ethanol 1.6–1.9 mM). The isozyme versus species differences mark the variability of class‐I alcohol dehydrogenase versus class III and suggest a parallelism between rapid mutational differences and frequent duplicatory events.

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Section: Tacacagacgccttccttggaagcagtcttcttctgattcctgtatcc~catcatctgtamentioning

confidence: 62%

Section: Proteinsmentioning

confidence: 99%

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confidence: 99%

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Isozyme developments in mammalian class‐I alcohol dehydrogenase

Höög

Vagelopoulos

Yip

et al. 1993

European Journal of Biochemistry

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“…Additionally, these data suggest that MAA is not likely to be the proximate toxicant inhibiting gap junctional communication be-cause MAA is the product of alcohol dehydrogenase. Although the enzyme isoforms present in a given system can alter 4-MP e¤cacy (Keung and Yip, 1989;Kassam et al, 1989;Nusrallah et al, 1989), the concentration of 4-MP used in this study is within the broad range of reported values for the dissociation constant of the enzyme^inhibitor complex (K i ). In these studies, K i values range from 0.11+0.03 mmol/ L in rat liver (Plapp et al, 1984) to 560 mmol/L in rat microsomes (Feierman and Cederbaum, 1986).…”

Section: Discussionmentioning

confidence: 93%

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Marty

Loch‐Caruso

1998

Cell Biology and Toxicology

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The glycol ethers 2-methoxyethanol (2-ME) and 2-ethoxyethanol (2-EE) prolong gestation in rodents. Because gap junctions in the myometrium likely facilitate parturition, the present study examined inhibition of gap junctional communication by 2-ME and 2-EE in myometrial smooth-muscle cell cultures. To measure gap junctional communication, the fluorescent dye Lucifer yellow was injected into cultured cells and the transfer of the dye to adjacent cells was scored with epifluorescence microscopy. The data are presented as the percentage of cells adjacent to the microinjected cell that exhibited dye following microinjection. A 30 min treatment with 32 or 63 mmol/L 2-ME decreased dye transfer to 71% and 63%, respectively (p < or = 0.05; control 90%). Similarly, 2-EE inhibited dye transfer, although myometrial cells were less sensitive to 2-EE compared to 2-ME. Dye transfer returned to control levels after 2 h in the continued presence of 2-ME. The primary metabolite of 2-ME, methoxyacetic acid (MAA), had no effect on dye transfer at concentrations equimolar to 2-ME. Because 2-ME and 2-EE inhibited gap junctional communication only at high concentrations and because the inhibition reversed in the continued presence of the compounds, it is suggested that glycol ethers delay parturition by a mechanism independent of a direct action on myometrial gap junctions.

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Alcohol dehydrogenase

Schomburg¹,

Stephan²

1995

Enzyme Handbook 9

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Rabbit liver alcohol dehydrogenase: Isolation and characterization of class I isozymes

Cited by 10 publications

References 19 publications

Isozyme developments in mammalian class‐I alcohol dehydrogenase

Isozyme developments in mammalian class‐I alcohol dehydrogenase

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Alcohol dehydrogenase

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