scholarly journals Reactivity and function of sulfhydryl groups in alanine dehydrogenase of Bacillus natto KMD 1126.

1980 ◽  
Vol 28 (5) ◽  
pp. 1503-1508 ◽  
Author(s):  
KATSUHIKO MATSUI ◽  
KIYOMI KIKUNO ◽  
YUKIO KAMEDA
Keyword(s):  
Sulfhydryl Groups ◽  
Bacillus Natto ◽  
Alanine Dehydrogenase ◽  
And Function

Comparison of the structure and function of ribulosebisphosphate carboxylase–oxygenase from a cold-hardy and nonhardy potato species

1981 ◽  
Vol 59 (4) ◽  
pp. 280-289 ◽  
Author(s):  
Norman P. A. Huner ◽  
Jiwan P. Palta ◽  
Paul H. Li ◽  
John V. Carter
Keyword(s):  
Large Subunit ◽  
Structure And Function ◽  
Sulfhydryl Groups ◽  
Relative Mass ◽  
Nitrobenzoic Acid ◽  
Significant Difference ◽  
Ribulosebisphosphate Carboxylase ◽  
Cold Hardy ◽  
And Function ◽  
Kinetics Of

A comparison of ribulosebisphosphate carboxylase–oxygenase from the leaves of the non-acclimated, cold-hardy species, Solanum commersonii, and the nonacclimated, nonhardy species, Solanum tuberosum showed that this enzyme from the two species differed in structure and function. The results of sulfhydryl group titration with 5,5′-dithiobis(2-nitrobenzoic acid) indicated that the kinetics of titration and the number of accessible sulfhydryl groups in the native enzymes were different. After 30 min, the enzyme from the hardy species had 1.7 times fewer sulfhydryl groups titrated than that from the nonhardy species. In the presence of 1% (w/v) sodium dodecyl sulfate, the total number of sulfhydryl groups titratable with 5,5′-dithiobis-(2-nitrobenzoic acid) was the same for both species. However, this denaturant had a differential effect on the kinetics of titration with 5,5′-dithiobis(2-nitrobenzoic acid). Both enzymes had a native molecular weight of about 550 000. The quaternary structures of the two enzymes were similar with the presence of large and small subunits of 54 000 and 14 000, respectively. However, there was more polypeptide of 108 000 – 110 000 present in preparations of the enzyme from S. tuberosum than from S. commersonii. This polypeptide is an apparent dimer of the large subunit on a relative mass basis. The large subunit of the enzyme from S. tuberosum was more sensitive to the absence of reducing agent and was more sensitive to freezing and thawing than the large subunit of the enzyme from S. commersonii. Catalytic properties of both enzymes at 5 and 25 °C indicated no significant difference in the [Formula: see text] at either temperature. However, the Vmax at 5 °C for the enzyme from S. commersonii was 35% higher than that of the enzyme from S. tuberosum. In contrast, the Vmax at 25 °C for the enzyme of the hardy species was 250% lower than that of the enzyme from the nonhardy species.

scholarly journals Purification and properties of alanine dehydrogenase from Bacillus natto KMD 1126.

1977 ◽  
Vol 25 (8) ◽  
pp. 2061-2066 ◽  
Author(s):  
KATSUHIKO MATSUI ◽  
YUKIKO TAMEGAI ◽  
AKIKO MIYANO ◽  
YUKIO KAMEDA
Keyword(s):  
Bacillus Natto ◽  
Alanine Dehydrogenase ◽  
Purification And Properties

Recombinant rat liver guanidinoacetate methyltransferase: reactivity and function of sulfhydryl groups

Biochemistry ◽  
1988 ◽  
Vol 27 (20) ◽  
pp. 7658-7664 ◽  
Author(s):  
Motoji Fujioka ◽  
Kiyoshi Konishi ◽  
Yoshimi Takata
Keyword(s):  
Rat Liver ◽  
Sulfhydryl Groups ◽  
And Function

Sulfhydryl Groups and Gastric Acid Secretion

1955 ◽  
Vol 184 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Horace W. Davenport ◽  
Virginia J. Chavré ◽  
Virginia D. Davenport
Keyword(s):  
Acid Secretion ◽  
Gastric Acid Secretion ◽  
Gastric Acid ◽  
Lipoic Acid ◽  
Enzyme System ◽  
Sulfhydryl Groups ◽  
Methyl Glyoxal ◽  
High Concentration ◽  
And Function ◽  
Stimulation Of

Gastric acid secretion is inhibited by reagents attacking sulfhydryl groups: iodoacetate amide (IAAm), N-ethyl maleimide (NEM), p-chloromercuribenzoate (ClHgB) and various forms of trivalent arsenic. An attempt was made to discover the nature of the group attacked by studying the effect of these and other reagents upon four sulfhydryl systems of the stomach: succinoxidase, glutathione (GSH), coenzyme A (CoA) and lipoic acid. Succinoxidase activity is reduced only slightly by treatment with IAAm or NEM which severely inhibits secretion. Both the enzyme system and secretion are inhibited by 2,3-dimercaptopropanol (BAL). Neither malonate nor succinate affects acid secretion or oxygen uptake under conditions designed to facilitate their entrance into cells. Succinoxidase activity in extracts of stomachs is only slightly if at all affected by prior stimulation of the stomach to secrete. GSH is reduced by IAAm or NEM. Addition of GSH does not reverse inhibition. GSH oxidase is absent from extracts, but the stomach reduces GSSG. Extracts contain methyl glyoxalase, but addition of crude methyl glyoxal inhibits acid secretion. CoA is reduced by NEM parallel with NEM's effect on secretion. IAAm has little effect on CoA. Addition of CoA does not reverse inhibition. Benemid inhibits acid secretion, and its effect is additive with that of NEM and 2,4-dinitrophenol. The lipoic acid content as assayed by S. faecalis is unaffected by IAAm or arsenite and only by high concentration of NEM. The effect of arsenite is strongly additive with that of the other inhibitors. Diphenylchloroarsine inhibits and is not reversed by GSH. No certain conclusions concerning the relation of metabolism and function can be drawn from this work.

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