Bloat in cattle

Clarke, R. T. J.; Jones, William T.; Reid, C. S. W.

doi:10.1080/00288233.1974.10421026

Cited by 12 publications

(1 citation statement)

References 10 publications

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“…Salivary mucoprotein (SMP) and oesophageal mucin (OSM) SMP and OSM were isolated from bovine salivary secretions as described previously (Lyttleton 1964;Clarke et al 1974). SMP was labelled with radioactive iodine (1251) (Marchalonis 1969 & Lyttleton 1972a) or by loss of soluble HC activity.…”

Section: Fraction 1 Leaf Proteinmentioning

confidence: 99%

I. Foam stabilising materials

Jones¹,

Lyttleton²,

Mangan

1978

New Zealand Journal of Agricultural Research

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Polygalacturonic acid and salivary macromolecules increased the persistence of Fraction [ leaf protein foams generated in vitro. The increase in persistence effected by polygalactmonic acid could be explained by increased bulk viscosity which decreased the foam drainage of the mixed foam. The effect of the salivary molecules, i.e., bovine salivary mucoprotein and oesophageal mucin, could not totally be explained by viscosity. A study of the reaction between salivary mucoprotein and Fraction 1 protein indicated a specific, non-ionic, pHuependent interaction between the molecules at sUlfaces only and not in solution.

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Section: Fraction 1 Leaf Proteinmentioning

confidence: 99%

I. Foam stabilising materials

Jones¹,

Lyttleton²,

Mangan

1978

New Zealand Journal of Agricultural Research

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The purification and characterization of bovine salivary proteins by electrophoretic procedures

1987

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Bovine salivary proteins have been shown to be correlated with bloat susceptibility in cattle. Due to the presence of the high molecular weight mucoprotein in whole saliva these proteins have been difficult to purify. This difficulty has now been overcome by using electrophoretic procedures. The purification protocol consisted of electrophoretic concentration ofthe saliva. separation of the proteins by polyacrylamide gel electrophoresis, excision of the protein bands followed by electroelution and concentration. Purified proteins were obtained from bands 4, 5 , 6 , 7,8 and 9/10. The molecular weights of the intact proteins were between 40 300 and 112 400 on gel chromatography and the subunit molecular weights were between 15 000 and 65 400. The isoelectric points were within the pH range of 3.6 to 5.1. Antisera were produced against protein bands 7 and 8 and these were used to determine antigenic relationships between proteins and as a means of quantifying the proteins by the Laurel1 rocket immunoassay.Abbreviations: CIUNITS, correctedintegrationunits: p2.isoelectric point; SEM, standard error of the mean: SDS. sodium dodecyl sulfate individual salivary gland ducts [21. Samples were centrifuged for 10 min at 1500 g and stored frozen.

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