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Biomedical subjects

J C Boursnell

Publications and source records attributed to J C Boursnell.

At least 19 recordsLinked to original sources
PubMed1981

Formation of a double salt of phosphatidylcholine and zinc chloride.

ZnCl2 forms a 1 : 1 double salt with phosphatidylcholine. This compound resembles the long-known double salt of CdCl2 and phosphatidylcholine except that the latter has the composition (CdCl2)3(phosphatidylcholine)2. Treatment of phosphatidylcholine with a mixture of equimolar amounts of ZnCl2 and CdCl2 yields the ZnCl2 double salt. The ZnCl2 double salt can be obtained as an amorphous flocculent precipitate and as small spherules. These results are discussed in relation to the toxic action of cadmium salts on the mammalian testis and to the protection afforded by zinc salts. It is suggested that membrane phospholipids are essential components of specific sites for reversible binding of Zn2+ and Cd2+.

Cadmium↗
PubMed1978

Effect of egg yolk and other reagents upon the zinc of cold-shocked boar spermatozoa.

A marked reduction (80.8%) in the zinc uptake by boar spermatozoa cooled to 4 degrees C occurs when the seminal plasma is pretreated with egg yolk-glucose at this temperature. Crude lecithin is less effective (59.8%). Similar pretreatment of the seminal plasma by the polycationic drug Antrypol, which totally removes the zinc-precipitable basic haemagglutinin, does not result in a significant reduction of the sperm zinc uptake at 4 degrees C.

Animals↗
PubMed1977

The constant ratio of the zinc content of boar spermatozoa of 4 degrees C and room temperature.

The ratio of the zinc content of boar spermatozoa obtained from semen cooled to 4 degrees C for 30 min to that of the original room temperature control (20-26 degrees C) was constant at 2-28 +/- 0-16 in 22 samples of fresh whole semen from 12 animals. The same ratio occurred when zinc (0 to 0.6 mM in citrate buffer) was added to semen or washed spermatozoa. The increase is dependent only on the initial sperm zinc content at room temperature.

Animals↗
PubMed1975

The split ejaculate of the boar: contributions of the epididymides and seminal vesicles.

The epididymal and seminal vesicular contributions to split-ejaculate fractions from boars were analysed for sperm concentration, glycerylphosphorylcholine (GPC), total-N, ethanol-soluble and insoluble N, citrate, zinc and haemagglutinin. The same components were also determined in epididymal plasma (EP), vesicular secretion (VS) and whole seminal plasma (SP). Isoelectric focusing of protein patterns was studied in the fractions. With the exception of haemagglutinin, the components were present to a major extent in either VS or EP and in lower concentrations in the other secretion. The parameters in VS or EP were positively correlated among themselves and negatively correlated with most of the parameters of the other fluid. The correlation coefficients were not significant in all cases for individual animals, but the degree of significance was greater for the over-all correlations. The EP components were mainly secreted in the first three or four fractions, but occasionally from fraction four onwards. Those of VS were emitted during the entire ejaculation, the maximum occurring in the sperm-rich fraction or the immediately succeeding fraction. The first fractions were devoid of VS components in only one case. The majority of the EP proteins could be identified electrophoretically in the sperm-rich fractions, but the protein patterns in the other fractions were similar to those of VS. The results are discussed and compared with previous findings.

Animals↗
PubMed1975

The isolation and characterization of lactoferrin from sow milk and boar seminal plasma.

Lactoferrin isolated from sow milk (about 0-6 mg/ml) was shown to be chromatographically homogeneous, an observation supported by electrophoresis and by reaction against monospecific anti-lactoferrin antiserum. Isoelectric focusing showed multiple forms of the protein (i.e.p., 9-3 to 10-0) converted by neuraminidase to one form (i.e.p., 9-65). Boar seminal plasma contains immunologically identical lactoferrin (0-1 to 0-5 mg/ml) which binds strongly to boar spermatozoa.

Ammonium Sulfate↗
PubMed1975

Boar seminal zinc-precipitable protein and the haemagglutinin.

About 30% of boar seminal plasma nitrogen is maximally precipitated at room temperature by 6 to 10 mM zinc in citrate solution at pH 8. A rise in the total nitrogen precipitated by 1 to 6 mM zinc is accompanied by a fall in the haemagglutinin titre of the supernatant fluid. At 6 mM zinc addition, 95% of the haemagglutinin is precipitated, but much of this is recoverable by re-solution of the zinc precipitate. Protein profile studies by gel-filtration chromatography of the zinc precipitate solution reveals a mixture of proteins, some of which are not by themselves zinc-precipitable.

Agglutinins↗