Multiple molecular forms of avian aldolases. II. Enzymic properties and amino acid composition of chicken (Gattus domesticus) breast muscle aldolase

Several properties of crystalline chicken (Gallus domesticus) breast muscle aldolase (fructose 1,6-diphosphate–D-glyceraldehyde 3-phosphate lyase, EC 4.1.2.13) were determined. The enzyme was found to have a broad pH optimum centered around pH 7.1 and to be remarkably stable over a wide pH range. The temperature coefficient Q10 is 2.6 in the range from 10 to 35 °C. The enzyme is stable at 48 °C for 10 min and almost completely inactivated at 55 °C. The apparent Michaelis constants for fructose 1,6-diphosphate and fructose 1-phosphate were 4.2 × 10−5 M and 1.7 × 10−2 M, respectively. The phosphate inhibitor constant (K1) was 5.5 × 10−3 M.Chicken breast muscle aldolase is similar to the rabbit enzyme in many of the above properties, although there are significant differences in heat stability and amino acid composition.

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Multiple Molecular Forms of Avian Aldolases. VI. Enzymatic Properties and Amino Acid Composition of Chicken Liver Aldolase and Comparative Immunochemical Properties

Canadian Journal of Biochemistry ◽

10.1139/o71-094 ◽

1971 ◽

Vol 49 (6) ◽

pp. 658-665 ◽

Cited By ~ 11

Author(s):

Ronald R. Marquardt

Keyword(s):

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Chicken Liver ◽

Molecular Forms ◽

Ph Optimum ◽

Muscle Enzyme ◽

Wide Ph Range ◽

Mammalian Liver ◽

Liver And Kidney

Several properties of pure chicken (Gallus domesticus) liver aldolase (fructose-1,6-diphosphate D-glycer-aldehyde-3-phosphate-lyase, EC 4.1.2.13) were determined. The enzyme shows a broad pH optimum peaking around pH 7.7, is stable over a wide pH range, and has a temperature coefficient Q10 of 2.3. The enzyme is stable at 48 °C for 10 min and is almost completely inactivated at 55 °C.The amino acid composition of pure chicken liver aldolase was determined. Its composition was compared with those of chicken muscle and chicken brain aldolases and with the corresponding rabbit aldolase enzymes.Antiserum was prepared against purified chicken liver aldolase and the immunological properties of aldolases from various tissues and species were examined. In the chicken, the antiserum has a very pronounced reaction with liver and kidney aldolases but only a weak cross-reaction with either the brain or the muscle enzyme. The antiserum readily cross-reacts with other avian liver aldolases (turkey and budgerigar) but not with mammalian liver aldolases (rat and rabbit).

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The β-glucosidase in the gut contents of the snail Achatina achatina

Biochemical Journal ◽

10.1042/bj1570381 ◽

1976 ◽

Vol 157 (2) ◽

pp. 381-387 ◽

Cited By ~ 10

Author(s):

G M Umezurike

Keyword(s):

Molecular Weight ◽

Heat Stability ◽

Molecular Forms ◽

Gut Contents ◽

Ph Optimum ◽

Optimum Ph ◽

Michaelis Constants ◽

Molecular Complexity ◽

Beta Glucosidase ◽

Digestive Glands

1. The enzyme beta-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) from the gut contents of active Achatina achatina exists in two molecular forms, beta-glucosidase C (mol.wt. about 82000) and D (mol.wt. about 41000). 2. Only the lower-molecular-weight species was found in the gut contents of aestivating snails or in extracts from their digestive glands and washed gut walls. 3. On re-activation of some aestivating snails, betion of ATP and Mg2+ to the isolated gut contents or to extracts from washed gut walls led to the formation of higher-molecular-weight forms of the enzyme, beta-glucosidase A (mol.wt. about 329000) and beta-glucosidase B (mol.wt. about 165000). 5. All these forms of the enzyme have similar pH optimum (pH 5.0-5.6). 6. The Michaelis constants (Km) and heat stability of the enzyme increased with increasing molecular complexity.

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Malate dehydrogenases in phototrophic purple bacteria. Thermal stability, amino acid composition and immunological properties

Biochemical Journal ◽

10.1042/bj2520595 ◽

1988 ◽

Vol 252 (2) ◽

pp. 595-600 ◽

Cited By ~ 9

Author(s):

M A Tayeh ◽

M T Madigan

Keyword(s):

Amino Acid ◽

Amino Acid Composition ◽

Malate Dehydrogenase ◽

Acid Composition ◽

Rhodospirillum Rubrum ◽

Rhodobacter Capsulatus ◽

Purple Bacteria ◽

Heat Stability ◽

Heat Stable ◽

Rhodomicrobium Vannielii

Purified malate dehydrogenases from four species of non-sulphur purple phototrophic bacteria were examined for their heat-stability, amino acid composition and antigenic relationships. Malate dehydrogenase from Rhodospirillum rubrum, Rhodobacter capsulatus and Rhodomicrobium vannielii (which are all tetrameric proteins) had an unusually high glycine content, but the enzyme from Rhodocyclus purpureus (which is a dimer) did not. R. rubrum malate dehydrogenase was extremely heat-stable relative to the other enzymes, withstanding 65 degrees C for over 1 h with no loss of activity. By contrast, malate dehydrogenase from R. vannielii lost activity above 35 degrees C, and that from R. capsulatus above 40 degrees C. Amino acid compositional relatedness and immunological studies indicated that tetrameric phototrophic-bacterial malate dehydrogenases were highly related to one another, but only distantly related to the tetrameric enzyme from Bacillus. This suggests that, despite differences in their thermal properties, the tetrameric malate dehydrogenases of non-sulphur purple bacteria constitute a distinct biochemical class of this catalyst.

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Differences in the amino acid composition of the breast muscle of wild and farmed pheasants

Czech Journal of Food Sciences ◽

10.17221/17/2011-cjfs ◽

2012 ◽

Vol 30 (No. 4) ◽

pp. 309-313 ◽

Cited By ~ 8

Author(s):

A. Brudnicki ◽

A. Kułakowska ◽

D. Pietruszyńska ◽

M. Łożyca-Kapłon ◽

J. Wach

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Nutritional Value ◽

Amino Acid Profile ◽

Breast Muscle ◽

High Quality ◽

Nutritional Values ◽

Biological Value

Numerous studies show the slaughter yield and also basic chemical composition of pheasant meat. The results reveal a higher biological value of the meat of pheasants which were fed naturally, in comparison to the meat of pheasants fed with commercial mixtures. In many countries, the pheasant is selected with the aim of producing high quality meat with very desirable nutritional values. There are only few publications on amino acid composition of pheasant meat. The knowledge of amino acid composition of pheasant meat can be used to determine its potential nutritional value. The amino acid compositions were compared of the meats of wild and farm pheasants. In the study, the following amino acids were determined: Asp, Thr, Ser, Glu, Pro, Gly, Ala, Val, Ile, Leu, Tyr, Phe, His, Lys, Arg. An improved amino acid profile was found in the breast muscle of pheasants kept at the farm in comparison with that of wild pheasants.  

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