The Response of the Bovine Kidney to Increasing Plasma Inorganic Phosphorous Concentrations

1974 ◽  
Vol 16 (1) ◽  
pp. 131-133 ◽  
Author(s):  
H.W. Symonds ◽  
R. Manston
Keyword(s):  
Bovine Kidney ◽  
Inorganic Phosphorous

Impact of Transfaunation of Rumen Ciliate Cultures on Physical Examination, Selected Serum Parameters and Milk Profile in Defaunated Lactating Dairy Goats

2020 ◽  
Keyword(s):  
Physical Examination ◽  
Mixed Culture ◽  
Pure Culture ◽  
Milk Fat ◽  
Mixed Cultures ◽  
Dairy Goats ◽  
Serum Parameters ◽  
Native Breed ◽  
Culture Duration ◽  
Inorganic Phosphorous

Rumen ciliates still have mysterious secrets and influences in ruminants. This study investigated the effect of transfaunation of pure and mixed cultures of rumen ciliates on physical clinical examination, selected serum parameters and milk profile in defaunated lactating dairy goats. A number of 8 Baladi native breed goats were randomly classified into two groups each one containing 4 goats. Pure culture group was transfaunated with 6 ml of pure culture of Holotricha spp., while mixed culture group was transfaunated with 6 ml of mixed culture of 81.85% Holotricha and 18.15% Ophryoscolex spp. once weekly for three consecutive weeks, after defaunation of both groups using 30 ml of 8% SLS for two consecutive days. Serum and milk samples were collected weekly for three successive weeks to study effect of type of ciliate culture, duration of transfaunation and their interaction. Results revealed that transfaunation of pure and mixed cultures of rumen ciliates had no effect on physical examination with minimal non-significant improvement of calcium, inorganic phosphorous, total protein and globulin in serum of defaunated goats. Transfaunation of pure or mixed cultures of rumen ciliates within three weeks could not improve significantly decreased milk fat % of defaunated goats without any effect on other measured milk profile parameters. It is concluded that further investigations on transfaunation without prior defaunation should be performed using different pure and mixed cultures of rumen ciliates for therapeutic and productive purposes.

RENAL RESEARCH INSTITUTE SYMPOSIUM: Effective Diffusion Volume Flow Rates (Qe) for Urea, Creatinine, and Inorganic Phosphorous (Qeu, Qecr, QeiP) During Hemodialysis

2003 ◽  
Vol 16 (6) ◽  
pp. 474-476 ◽  
Author(s):  
Frank A. Gotch ◽  
Froilan Panlilio ◽  
Olga Sergeyeva ◽  
Laura Rosales ◽  
Tom Folden ◽  
...  
Keyword(s):  
Effective Diffusion ◽  
Volume Flow ◽  
Flow Rates ◽  
Inorganic Phosphorous ◽  
Research Institute

scholarly journals Purification and properties of 2-aminoadipate: 2-oxoglutarate aminotransferase from bovine kidney

1989 ◽  
Vol 261 (3) ◽  
pp. 761-768 ◽  
Author(s):  
D R Deshmukh ◽  
S M Mungre
Keyword(s):  
Rat Kidney ◽  
Deae Cellulose ◽  
Dicarboxylic Acids ◽  
Structural Similarity ◽  
Appreciable Amount ◽  
Kinetic Properties ◽  
Bovine Kidney ◽  
Purification And Properties ◽  
Kidney Enzyme ◽  
Structural Differences

Previous studies with rat kidney preparations indicated that 2-aminoadipate aminotransferase (AadAT) and kynurenine aminotransferase (KAT) activities are properties of a single protein. We found that bovine kidney contains an appreciable amount of AadAT activity, but lacks KAT activity. AadAT from bovine and rat kidney extracts were purified to electrophoretic homogeneity. The purification procedure included fractionation with (NH1)2SO1, heat treatment, DEAE-cellulose chromatography and hydroxyapatite chromatography. Physical and kinetic properties, such as pH optima, Km for substrates, Mr, electrophoretic mobility and inhibition by dicarboxylic acids of bovine kidney AadAT, were similar to those of the rat kidney enzyme. However, bovine kidney AadAT differed from rat kidney AadAT in substrate specificity, amino acid composition and stability when stored. The titration curve of bovine kidney AadAT was also different from that of the rat kidney enzyme. The results suggest that bovine kidney AadAT may have some structural similarity to rat kidney AadAT and that the structural differences observed between the two enzymes may explain the absence of KAT activity in bovine kidney.

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