Adaptation of cattle to tannins: rôle of proline-rich proteins in oak-fed cattle
- 1 October 1998
- journal article
- research article
- Published by Cambridge University Press (CUP) in Animal Science
- Vol. 67 (2), 277-281
- https://doi.org/10.1017/s1357729800010031
Abstract
Saliva and faecal samples were collected from hill cattle (no. = 10) given tannin-rich oak (Quercus incana) leaves in the north-west Himalayan region of India. Amino acid composition of the saliva samples after thawing to remove precipitated proteins by centrifugation, and dialysis (molecular weight cut off: 3500) to remove small moieties revealed 6·4 (s.d. 0·6) % proline, 15·6 (s.d. 0·6) % glutamine plus glutamate and 9·2 (s.d. 1·0) % glycine on molar basis. For Holstein Friesian cattle (no. = 4) which had no history of consumption of tannin-containing foods, these values were 6·5 (s.d. 0·4) %, 15·2 (s.d. 0·5) % and 9·8 (s.d. 0·7) % respectively. Proline concentration in the proteins present either as free or as tannin-protein complexes in the lyophilized faecal samples from hill cattle was 4·7 (s.d. 0·2) % (on molar basis) of the total amino acids and 5·3 (s.d. 0·2) % in Holstein Friesian cattle. In the faeces of oak-fed cattle, the tannin and condensed tannin levels on dry-weight basis were 0·81 (s.d. 0·20) % as tannin acid equivalent and 0·06 (s.d. 0·04) % as leucocyanidin equivalent respectively. For tannic acid, the relative affinity of salivary proteins, using the competitive binding assay, was about six-times higher than that of bovine serum albumin (BSA) and was of the same order as that of gelatin. Turbidity of complexes formed between salivary proteins or BSA and tannic acid showed proportionately about 0·50 lower turbidity for salivary proteins in 0-2 mol/I acetate buffer (pH 4·9 containing 0·17 mol/l NaCl) and proportionately about 0·84 lower turbidity in distilled water. The results suggest that unlike rats or mice, the proline-rich proteins do not appear to be of any physiological significance in the adaptation of cattle to tannins. However, the salivary proteins of cattle though not rich in proline, have a high affinity for tannins and these proteins have a high tendency to form soluble tannin-protein complexes.Keywords
This publication has 28 references indexed in Scilit:
- Salivary proline-rich proteins in mammals: Roles in oral homeostasis and counteracting dietary tanninJournal of Chemical Ecology, 1995
- Role of Condensed Tannin on Salivary Tannin-Binding Proteins, Bioenergetics, and Nitrogen Digestibility in Microtus pennsylvanicusJournal of Mammalogy, 1994
- Experience early in life affects voluntary intake of blackbrush by goatsJournal of Chemical Ecology, 1991
- Appraisal of four pre-column derivatization methods for the high-performance liquid chromatographic determination of free amino acids in biological materialsJournal of Chromatography A, 1990
- Tannin-binding proteins in saliva of deer and their absence in saliva of sheep and cattleJournal of Chemical Ecology, 1989
- Dietary Tannins and Salivary Proline-Rich Proteins: Interactions, Induction, and Defense MechanismsAnnual Review of Nutrition, 1987
- Use of dye-labeled protein as spectrophotometric assay for protein precipitants such as tanninJournal of Chemical Ecology, 1985
- The Binding of Dietary Protein by Sorghum Tannins in the Digestive Tract of PigsJournal of Nutrition, 1984
- Principles of Protein StructureSpringer Advanced Texts in Chemistry, 1979
- Protein precipitation method for the quantitative determination of tanninsJournal of Agricultural and Food Chemistry, 1978