Bovine testes

The fluorescence of the two tyrosine residues in bovine testes calmodulin was investigated by Pundak and Roche.(123) Upon excitation at 278 nm, a second emission, in addition to tyrosine fluorescence, was observed at 330-355 nm, which they characterized as being due to tyrosinate fluorescence. The tyrosinate fluorescence appeared to be from Tyr-99, which has an anomalously low pKa of about 7 for the phenol side chain. Pundak and Roche(123) reasoned that since tyrosinate emission is apparently not being seen in other species of calmodulin, it is possible that the bovine protein contains a carboxylate side chain in domain III which is amidated in other species. They further argued that the tyrosinate emission from bovine testes calmodulin arises from direct excitation of an ionized tyrosine residue. This tyrosinate fluorescence is discussed in more detail in Section 1.5.2. 

The tyrosinate fluorescence observed with bovine testes calmodulin is argued to be due to tyrosinate in the ground state.(123) Of the two tyrosine residues in this calmodulin, Tyr-99 apparently has a low pKa near 7 for the formation of tyrosinate, which is most likely due to nearby side chains that are involved in calcium binding. These groups could then also account for the complex pH dependence of the 345-nm emission intensity. Besides the tyrosine and tyrosinate emissions at 305 and 345 nm, respectively, Pundak and Roche(123) also reported the existence of a third emission band between 312 and 320 nm. This band was similar in its pH and calcium dependence to the other residue, Tyr-138, and was speculated to be a result of a combination of contributions from the tyrosine and tyrosinate emissions. Since this band has its excitation profile shifted to the red, however, it could be that a hydrogen-bonded tyrosine exists in this calmodulin. Alternatively, it has also been found that the presence of the 345-nm emission depends upon the method of preparation (G. Sanyal, personal communication). 

S. Pundak and R. S. Roche, Tyrosine and tyrosinate fluorescence of bovine testes calmodulin Calcium and pH dependence, Biochemistry 23, 1549-1555 (1984). 

B-Galatosidase (from bovine testes). Purified 600-fold by ammonium sulphate precipitation, acetone fractionation and affinity chromatography on agarose substituted with terminal thio-6-galactopyranosyl residues. [Distlem and Jourdian JBC 248 6172 1973. ... 

Wrobel, K.-H., Bickel, D., and Kujat, R. 1996. Immunohistochemical study of seminiferous epithelium in adult bovine testes using monoclonal antibodies against Ki-67 protein and proliferating cell nuclear antigen (PCNA). Cell Tissue Res. 283 191-201. 

Orchic substance (bovine) — Extract from bovine testes used to increase testosterone... 

ANALYSIS OF INHIBITOR GLYCOPROTEINS FROM BOVINE TESTES EXTRACT... 

Thrombin Time (TT). To 0.1 ml of citrated plasma 0.1 ml of diethylbarbiturate-citrate buffer, pH 7.6 (Behring Werke, Marburg) is added and the mixture is incubated for 1 min at 37 °C. Then 0.1 ml of bovine test-thrombin (30 IU/ml, Behring Werke, Marburg) is added and the coagulometer is started. The time to clot formation is determined. The TT measures effects on fibrin formation. 

Membrane preparations from bovine testes are used according to the methods of Cheng (1975) and Andersen (1983). Fresh bovine testes or testes from rats weighing 220-280 g are decapsulated and rinsed with cold 0.025 M Tris-HCl buffer at pH 7.2, containing 0.3 M sucrose, and then minced and homogenized with a Polytron homogenizer at maximum speed for 30 sec at a concentration of 5 ml buffer per g of tissue. The... 

In another case, Thiem et al. used a fS-galactosidase from bovine testes in the transfer of a galactose from lactose to glucose or galactose-containing structures with yields ranging from 7% to 44% (16). The enzyme showed a preference for the formation of fSl,3-linkage. 

Schroder S, Schmidt U, Thiem J, Kowalczyk J, Kunz M, Vogel M. Synthesis of oligosaccharides as potential novel food 32. components and upscaled enzymatic reaction employing the P-galactosidase from bovine testes. Tetrahedron 2004 60 2601-... 

The highest PA-PLAi activity was observed in high speed supernatant fractions from homogenates of bovine testes and brain, with little or no activity in corresponding fractions from newborn testes, liver, spleen, heart, and blood [46]. A northern blot analysis of mRNA from human tissues agreed with the observations with bovine tissues [16]. 

The molecular mass of the expressed PA-PLAi was estimated to be 110 kDa by SDS-PAGE, and 97.6 kDa by matrix-associated laser desorption/ionization [48]. A value of 97.6 kDa was also obtained from the deduced amino acid sequence of the open reading frame (ORF) [48]. The enzyme purified from bovine testes had an apparent molecular mass of 440 kDa, as determined by size exclusion chromatography [48], suggesting that PA-PLAi exists as a homotetramer of 98 kDa subunits in solution. The molecular mass of bovine brain PA-PLAi, estimated by the same method, was 200 kDa, suggesting that it exists as a homodimer in the brain [48]. 

PA-PLAi, which is expressed in mature bovine testes but not in newborn calf testes, may contribute to the formation or function of sperm. PA-PLAi may also be involved in the remodebng of phospholipids by hydrolyzing fatty acids at the sn-1 position and by subsequent acylation that occurs at this position. 

Disaccharide 16.25 is first made by tran -galactosylation in the presence of a /3-gaIactosidase from bovine testes, according to reaction (16.1). This is followed by sialylation in the presence of ST3 sialyltransferase from porcine liver, according to reaction (16.2). CMPNeuSAc was regenerated by the multi-enzyme system described in Section 12,4. 

Figure 3 Inhibition properties of some flavonoids (250 mM) on hyaluronidase from several venom sources and from bovine testes. (From Refs. 80,81.)...

B. Fiszer-Szafarz. Hyaluronidase polymorphism detected by polyacrylamide gel electrophoresis. Application to hyaluronidases from bacteria, slime molds, bee and snake venoms, bovine testes, rat liver lysosomes and human serum. Anal. Biochem. 143 16 (1984). 

Hyaluronidase is an enzyme extracted from mammalian testes (e.g., bovine testes) and capable of hydrolyzing mucopolysaccharides of the hyaluronic acid type. It contains not less than 3001.U. of hyaluronidase activity per milligram, calculated with reference to the dried substance. It may contain a suitable stabilizer. 

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