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1.
Vet Rec ; 99(11): 210-2, 1976 Sep 11.
Article in English | MEDLINE | ID: mdl-969181

ABSTRACT

Long term experiments were carried out to determine the influence of varying energy intakes on the levels of blood components in lactating beef cows. Lowering the dietary energy intake to 0-95x maintenance produced a fall in bodyweight which continued throughout a 10 week feeding period. There was an initial fall in the plasma glucose level. After four weeks the plasma glucose level began to rise, and at the end of the 10 week period it had almost reached its original level. When bodyweight and plasma glucose were falling cows were infertile, when bodyweight was falling and plasma glucose was rising cows were fertile.


Subject(s)
Blood Glucose/analysis , Body Weight , Cattle/physiology , Fertility , Animals , Cattle/metabolism , Diet , Energy Metabolism , Female , Fertilization , Pregnancy
2.
J Sci Food Agric ; 27(6): 520, 1976 Jun.
Article in English | MEDLINE | ID: mdl-972525
10.
Biochem J ; 106(1): 135-40, 1968 Jan.
Article in English | MEDLINE | ID: mdl-5721453

ABSTRACT

1. The previous study (Conchie, Gelman & Levvy, 1967b) of the specificity of beta-glucosidase, beta-galactosidase and beta-d-fucosidase in barley, limpet, almond emulsin and rat epididymis was extended to alpha-l-arabinosidase. 2. The inhibitory action of l-arabinono-(1-->5)-lactone was tested against all four types of enzyme, and alpha-l-arabinosidase was examined for inhibition by glucono-, galactono- and d-fucono-lactone. 3. In emulsin, the enzyme that hydrolyses beta-glucosides, beta-galactosides and beta-d-fucosides also hydrolyses alpha-l-arabinosides. Rat epididymis resembles emulsin except that, as already noted, it lacks beta-glucosidase activity. 4. In the limpet, alpha-l-arabinosidase activity is associated with the enzyme that hydrolyses beta-glucosides and beta-d-fucosides, and not with the separate beta-galactosidase. 5. The effects of the different lactones on the barley preparation suggest that alpha-l-arabinosidase activity is associated with the beta-galactosidase rather than with the enzyme that hydrolyses beta-glucosides and beta-d-fucosides. Fractionation and heat-inactivation experiments indicate that there is also a separate alpha-l-arabinosidase in the preparation.


Subject(s)
Arabinose , Glycoside Hydrolases/antagonists & inhibitors , Lactones , Aldehydes , Animals , Edible Grain/enzymology , Epididymis/enzymology , Fucose , Galactose , Galactosidases/antagonists & inhibitors , Glucose , Glucosidases/antagonists & inhibitors , Glycoside Hydrolases/analysis , Kinetics , Male , Mollusca/enzymology , Nuts , Rats
11.
Biochem J ; 103(3): 609-15, 1967 Jun.
Article in English | MEDLINE | ID: mdl-6069163

ABSTRACT

1. In barley, beta-glucosidase and beta-galactosidase are separate enzymes. The former also displays beta-d-fucosidase activity. 2. In the limpet, Patella vulgata, beta-glucosidase activity is associated with the beta-d-fucosidase, previously shown to be a separate entity from the beta-galactosidase also present. 3. Almond emulsin presents all three activities as a single enzyme. Each is equally inhibited by glucono-, galactono- and d-fucono-lactone. 4. In rat epididymis, there is no significant beta-glucosidase activity, nor is there appreciable inhibition of the beta-galactosidase and beta-d-fucosidase activities of the preparation by gluconolactone.


Subject(s)
Galactosidases/metabolism , Glucosidases/metabolism , Lactones/metabolism , Animals , Edible Grain/enzymology , Epididymis/enzymology , Galactosidases/antagonists & inhibitors , Glucosidases/antagonists & inhibitors , Glycosides/metabolism , Hydrogen-Ion Concentration , Kinetics , Male , Mollusca
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