Rumen Chemistry, In Vitro Studies with Rumen Microorganisms Using Carbon-14-Labeled Casein, Glutamic Acid, Leucine, and Carbonate

1955 ◽  
Vol 3 (11) ◽  
pp. 948-951 ◽  
Author(s):  
K. K. Otagaki ◽  
A. L. Black ◽  
Harold Goss ◽  
Max Kleiber
Keyword(s):  
Glutamic Acid ◽  
In Vitro Studies ◽  
Rumen Microorganisms ◽  
Carbon 14

The metabolism of acetate by rumen microorganisms

1974 ◽  
Vol 20 (2) ◽  
pp. 183-185 ◽  
Author(s):  
B. Emmanuel ◽  
L. P. Milligan ◽  
B. V. Turner
Keyword(s):  
Amino Acids ◽  
Fatty Acids ◽  
Nucleic Acids ◽  
Glutamic Acid ◽  
Acetate Metabolism ◽  
Rumen Microorganisms ◽  
Wide Range

Rumen contents were incubated in vitro with acetate-1-14C. Significant amounts of 14C were incorporated into rumen microbial proteins, nucleic acids, and lipids. Serine, glutamic acid, methionine, and cystine were highly labeled, whereas less, or insignificant radioactivity was found in other amino acids. Acetate was incorporated into a wide range of microbial fatty acids. The quantitative significance of acetate metabolism is discussed.

scholarly journals Pathogenic Roles of Glutamic Acid Decarboxylase 65 Autoantibodies in Cerebellar Ataxias

2017 ◽  
Vol 2017 ◽  
pp. 1-12 ◽  
Author(s):  
Hiroshi Mitoma ◽  
Mario Manto ◽  
Christiane S. Hampe
Keyword(s):  
Glutamic Acid ◽  
Glutamic Acid Decarboxylase ◽  
In Vitro Studies ◽  
Acid Decarboxylase ◽  
Pathogenic Role ◽  
Cerebellar Ataxias ◽  
Glutamic Acid Decarboxylase 65

Reports suggesting a pathogenic role of autoantibodies directed against glutamic acid decarboxylase 65 (GAD65Abs) in cerebellar ataxias (CAs) are reviewed, and debatable issues such as internalization of antibodies by neurons and roles of epitopes are discussed. GAD65 is one of two enzymes that catalyze the conversion of glutamate to the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). A pathogenic role of GAD65Ab in CAs is suggested by in vivo and in vitro studies. (1) Intracerebellar administration of cerebrospinal fluid (CSF) immunoglobulins (IgGs) obtained from GAD65Ab-positive CA patients impairs cerebellar modulation of motor control in rats. (2) CSF IgGs act on terminals of GABAergic neurons and decrease the release of GABA in cerebellar slices from rats and mice. (3) Absorption of GAD65Ab by recombinant GAD65 diminishes the above effects, and monoclonal human GAD65Ab (b78) mimic the effects of CSF IgGs in vivo and in vitro. Studies using GAD65-KO mice confirm that the target molecule is GAD65. (4) Notably, the effects of GAD65Ab depend on the epitope specificity of the monoclonal GAD65Ab. Taken together, these results indicate that epitope-specific GAD65Ab-induced impairment of GABA release is involved in the pathogenesis of GAD65Ab-positive CA and support the early detection of GAD65Ab-associated CA to initiate immunotherapy before irreversible neuronal death in the cerebellum.

DEGRADATION OF MIMOSINE IN RUMEN FLUID FROM CATTLE AND SHEEP IN CANADA

1984 ◽  
Vol 64 (4) ◽  
pp. 937-942 ◽  
Author(s):  
H. KUDO ◽  
K.-J. CHENG ◽  
W. MAJAK ◽  
J. W. HALL ◽  
J. W. COSTERTON
Keyword(s):  
Amino Acid ◽  
Key Words ◽  
Leucaena Leucocephala ◽  
Rumen Fluid ◽  
Average Rate ◽  
In Vitro Studies ◽  
Rumen Microorganisms ◽  
Microbial Detoxification ◽  
Cattle And Sheep

The microbial detoxification of mimosine was detected during in vitro studies with rumen fluid from cattle and sheep in Canada. The toxic amino acid, a component of Leucaena leucocephala (Leguminosae), was degraded rapidly (average rate 2.17 μg∙mL−1∙h−1) by rumen inocula from sheep on a concentrate diet but inocula from sheep on cubed hay showed much less activity (0.44 μg∙mL−1∙h−1). Mimosine was also metabolized by rumen microorganisms from steers on concentrate rations (2.88 μg∙mL−1∙h−1) but rates were lower when inocula originated from cattle fed hay, pasture or silage diets (< 1.87 μg∙mL−1∙h−1). Our results show that in Canada, rumen fluid contains microorganisms capable of mimosine degradation and that the rates of detoxification are enhanced by rumen microbiota from sheep and cattle on concentrate diets. Key words: Detoxification, rumen microorganisms, mimosine, sheep, cattle

In vitro - studies with antler bone cells: Structure forming capacity, osteocalcin production and influence of sex steroids

2006 ◽  
Vol 15 (04) ◽  
pp. 245-257 ◽  
Author(s):  
H. J. Rolf ◽  
K. G. Wiese ◽  
H. Siggelkow ◽  
H. Schliephake ◽  
G. A. Bubernik
Keyword(s):  
Sex Steroids ◽  
Bone Cells ◽  
In Vitro Studies ◽  
Osteocalcin Production

In Vitro Studies on the Mechanism of the Antifibrino-lytic Action of E-Aminocaproic Acid (EACA)

1968 ◽  
Vol 19 (03/04) ◽  
pp. 584-592 ◽  
Author(s):  
Hanna Lukasiewicz ◽  
S Niewiarowski
Keyword(s):  
Aminocaproic Acid ◽  
Test Tube ◽  
In Vitro Studies ◽  
Lytic Action ◽  
Human Plasminogen ◽  
Experimental Findings ◽  
Fibrin Clots

Summary and Conclusion1. It has been found that EACA does not inhibit activation of human plasminogen into plasmin by SK and UK in a concentration of 5 × 10–2 M. The activation of bovine plasminogen by SK and UK is inhibited by this concentration of EACA but not by a lower one.2. EACA in concentrations of 1,5 × 10–1 – 10–4 M does not inhibit casein proteolysis by plasmin. The proteolysis of fibrinogen and fibrin measured by the release of TCA soluble tyrosine is inhibited by EACA in concentrations of 1,5 × 10–1 – 10–2 M.3. The lysis of non-stabilized clots by plasmin measured in a test tube was inhibited by an EACA concentration of 5 × 10–3 – 5 × 10–4 M. The lysis of stabilized clots by plasmin was inhibited by an EACA concentration of 10–5 M.4. On the basis of experimental findings and data given in literature the authors postulate that the mechanism of the antifibrinolytic effects of EACA consists mainly in a modification of plasmin action on fibrin. These effects are dependent on the structure of the fibrin clots.

The Venom of the Boomslang (Dispholidus Typus): In Vivo and in Vitro Studies

1969 ◽  
Vol 21 (02) ◽  
pp. 234-244 ◽  
Author(s):  
N Mackay ◽  
J.C Ferguson ◽  
Antonia Bagshawe ◽  
A.T.T Forrester ◽  
G.P Mcnicol
Keyword(s):  
In Vitro Studies

SummaryAn account is given of the effects of boomslang venom in man. Evidence was found of a fibrinolytic state apparently secondary to the coagulant action of the venom. These features rapidly responded to the administration of specific antivenom. In vitro studies, using a homogenate of boomslang parotids, confirmed the coagulant properties of the venom and showed them to be of much greater potency than the proteolytic actions.

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