Evolution of the alcohol dehydrogenase (ADH) genes in yeast: characterization of a fourth ADH in Kluyveromyces lactis

1992 ◽  
Vol 232 (3) ◽  
pp. 479-488 ◽  
Author(s):  
Daniel H. Shain ◽  
Christopher Salvadore ◽  
Clyde L. Denis
Keyword(s):  
Alcohol Dehydrogenase ◽  
Kluyveromyces Lactis ◽  
Adh Genes

Isolation and characterization of alcohol dehydrogenase cDNAs from Pinusradiata

1990 ◽  
Vol 20 (9) ◽  
pp. 1343-1350 ◽  
Author(s):  
C. S. Kinlaw ◽  
D. E. Harry ◽  
R. R. Sederoff
Keyword(s):  
Alcohol Dehydrogenase ◽  
Southern Blot Analysis ◽  
Amino Acid Sequences ◽  
Coding Region ◽  
Coding Sequences ◽  
The Third ◽  
Isolation And Characterization ◽  
Adh Genes ◽  
Restriction Fragment Pattern

Three alcohol dehydrogenase (ADH) cDNAs were isolated from Pinusradiata. Two of the cDNAs appear to correspond to alleles of one ADH locus, and the third cDNA appears to correspond to a second ADH locus. Nucleotide and amino acid sequences of the coding region of ADH genes from the following species were compared: Pinusradiata, Zeamays, Hordeumvulgare, Triticumaestivum, Oryza sativa, Pisumsativum, and Arabidopsisthaliana. A phylogenetic tree was constructed of coding sequences of pine and angiosperm ADH genes. This tree shows three plant ADH clusters: monocot, dicot, and pine. The distance between pine and the two angiosperms is only slightly greater than the distance between either angiosperm, supporting the fossil evidence that suggests that monocots and dicots diverged from each other shortly after angiosperms diverged from gymnosperms. The structure of pine ADH genes was investigated by Southern blot analysis. The restriction fragment pattern of ADH genes from pines is more complex than the pattern from angiosperm genes, suggesting that pine ADH genes are either larger or more numerous than their angiosperm counterparts.

Partial characterization of cheese-ripening proteinases produced by the yeastKluyveromyces lactis

1983 ◽  
Vol 50 (4) ◽  
pp. 469-480 ◽  
Author(s):  
Paul A. Grieve ◽  
Barry J. Kitchen ◽  
John R. Dulley ◽  
John Bartley
Keyword(s):  
Molecular Weight ◽  
Kluyveromyces Lactis ◽  
Apparent Molecular Weight ◽  
Aminopeptidase Activity ◽  
Carboxypeptidase Y ◽  
Casein Hydrolysis ◽  
Cheese Ripening ◽  
Caseinolytic Activity ◽  
Proteinase A

SUMMARYAn extract ofKluyveromyces lactis416 and a β-galactosidase preparation (Maxilact 40000) contaminated with proteinase, showed similar pH profiles of caseinolytic activity. Similar modes of casein hydrolysis (κ-, > αs-, ≥ β-) were observed at pH 5·0 (the pH of Cheddar cheese), without detection of bitterness. The contaminated Maxilact preparation contained similar proteinase types to those detected in an autolysate ofK. lactis. Both the autolysate and the Maxilact preparation contained acid endopeptidase (proteinase A), serine endopeptidase (proteinase B) and serine exopeptidase (carboxypeptidase Y) activities. Some aminopeptidase activity was also detected in both preparations. There were some differences in apparent molecular weight and charge properties between proteinase A and B and carboxypeptidase Y from the 2 proteinase sources.

Thermodynamics of Adsorption of Alcohol Dehydrogenase on Gold Nanoparticle Surface: A Model Based Analysis Versus Direct Measurement

2021 ◽  
Author(s):  
Akriti Mishra ◽  
Kamini Mishra ◽  
Dipayan Bose ◽  
Abhijit Chakrabarti ◽  
Puspendu Kumar Das
Keyword(s):  
Alcohol Dehydrogenase ◽  
Gold Nanoparticle ◽  
Protein Interaction ◽  
Protein Corona ◽  
Quality Data ◽  
Nanoparticle Surface ◽  
Tremendous Importance ◽  
Good Quality Data ◽  
Model Based Analysis

Characterization of nanoparticle protein corona has gained tremendous importance lately. The parameters which quantitatively establish a specific nanoparticle-protein interaction need to be measured accurately since good quality data is necessary...

scholarly journals Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosu s

2001 ◽  
Vol 268 (10) ◽  
pp. 3062-3068 ◽  
Author(s):  
John van der Oost ◽  
Wilfried G. B. Voorhorst ◽  
Servé W. M. Kengen ◽  
Ans C. M. Geerling ◽  
Vincent Wittenhorst ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Biochemical Characterization ◽  
Short Chain ◽  
Chain Alcohol ◽  
Hyperthermophilic Archaeon ◽  
Short Chain Alcohol

Spectroelectrochemical Characterization of Quinohemoprotein Alcohol Dehydrogenase fromGluconobacter suboxydans

1997 ◽  
Vol 26 (6) ◽  
pp. 525-526 ◽  
Author(s):  
Masaki Torimura ◽  
Kenji Kano ◽  
Tokuji Ikeda ◽  
Teruhisa Ueda
Keyword(s):  
Alcohol Dehydrogenase
Sign in / Sign up

Export Citation Format

Share Document