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Lactoferrin and Transferrin in Bovine Milk in Relation to Certain Physiological and Pathological Factors P

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Lactoferrin and Transferrin in Bovine Milk in Relation to Certain Physiological and Pathological Factors P LACTOFERRIN AND TRANSFERRIN IN BOVINE MILK IN RELATION TO CERTAIN PHYSIOLOGICAL AND PATHOLOGICAL FACTORS P. Rainard, B. Poutrel, J.P. Caffin To cite this version: P. Rainard, B. Poutrel, J.P. Caffin. LACTOFERRIN AND TRANSFERRIN IN BOVINE MILK IN RELATION TO CERTAIN PHYSIOLOGICAL AND PATHOLOGICAL FACTORS. Annales de Recherches Vétérinaires, INRA Editions, 1982, 13 (4), pp.321-328. hal-00901388 HAL Id: hal-00901388 https://hal.archives-ouvertes.fr/hal-00901388 Submitted on 1 Jan 1982 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. LACTOFERRIN AND TRANSFERRIN IN BOVINE MILK IN RELATION TO CERTAIN PHYSIOLOGICAL AND PATHOLOGICAL FACTORS P. RAINARD B. POUTREL J.P. CAFFIN Institut National de la Recherche Agronomique, Station de Pathologie de la Reproduction, 37380 Nouzilly, France Résumé LACTOFERRINE ET TRANSFERRINE DANS LE LAIT EN RAPPORT AVEC CERTAINS FACTEURS PHYSIOLOGIQUES ET PATHOLOGIQUES. &horbar; Les concentrations moyennes de transferrine et de lactoferrine dans le lactosérum de 376 quartiers non-infectés de 42 vaches Holstein x Frisonne prélevé les 30°, 150. et 2701 jours de lactation ont été de 0,030 et 0,080 mg/ml respectivement. La concentration moyenne de transferrine dans le sérum a été de 4,63 mg/ml. Le nombre de lactation et la position des quartiers n’ont pas influencé les valeurs de lactoferrine et de transferrine dans le lait. La concentration de lactoferrine a augmenté significativement (P<0,01) dans les quartiers non-infectés, passant de 0,03 à 0,06 et à 0,15 mg/ml lors des trois prélèvements successifs. La concentration de transferrine dans le lactosérum n’a augmenté significativement (P<0,01) qu’en fin de lactation, passant de 0,025 (30’ et 150. jours de lactation) à 0,035 mg/ml (270° jour de lactation). La concentration de lactoferrine a augmenté significativement (P<0,01) dans les quartiers infectés par des pathogènes majeurs (41 échantillons), tandis que les infections dues aux pathogènes mineurs n’ont pas provoqué d’augmentation significative. Les valeurs 0,42 et 0,65 ont été trouvées pour les coefficients de corrélation entre les concentrations de lactoferrine et de transferrine dans le lait et le nombre de cellules somatiques, respectivement. Penetration into the mammary gland by and Viljoen, 19741 as well as other proteins such pathogenic bacteria provokes an inflammatory as a-lactalbumin and (3-casein and other el- reaction which manifests itself by numerous ements such as lactose (review by Kitchen, modifications in milk, which are not always 1981). evident, particularly in the case of subclinical and latent mastitis. The problem of diagnosis of non- However, some of the biochemical modifica- clinical mastitis by methods other than bacterio- tions to the milk’s composition are in direct logical ones has brought numerous authors to relation with the defense mechanisms which the study the variations in the chemical composition udder can mobilize in order to face a bacterial of milk. In particular the serum albumin (Giesecke attack. Increased passage of blood proteins towards the milk and stimulation of the local Bacteriological analysis synthesis of antibacterial factors have been An aliquot (25 pl) of a milk sample was spread reported (Carroll et al., 1963 ; Harmon et al., with a calibrated loop on esculine blood agar 1976 ; Hill et al., 1979). As well as the immuno- plate. Bacteria were identified after 24 and 48 h and the complement system, two globulins incubation at 37 °C (Plommet, 1962). proteins, due to their ability to bind firmly with Quarter infection status was as ferric iron, have an antibacterial action and are categorized follows : present in milk : transferrin which comes from the blood and lactoferrin which is synthetized by - No infection : no bacteria isolated from the the glandular epithelium (Harmon et al., 1976). quarter Their bacteriostatic effect on many bacteria has - Minor pathogen infection : Corynebacterium been well documented (review by Bullen et al., bovis, micrococci isolated 1978), and in certain conditions LF can exert a - Major pathogen infection : Staphylococcus bactericidal effect (Arnold et al., 1977). By aureus, streptococci, Corynebacterium pyoge- consequence, the appreciation of their role in the nes, coliform, yeast isolated defense of the mammary gland merits considera- tion. Somatic cell counting This study is aimed at investigating variations The recommended International in the concentration of lactoferrin and transferrin procedure by Federation 1979) was followed. in milk in relation to inflammation of the udder. Dairy (IDF, was performed with a Coulter counter This assessment firstly requires an evaluation of Counting (Model Coultronics, France) cali- the normal physiological variations of these F., Margency, brated with standard milk (from values. In this aim,variations in concentration of monthly samples INRA, France). the two proteins in non-infected glands were Poligny, investigated and related to certain physiological parameters such as age and stage of lactation. Preparation of lactoferrin The influence of subclinical mastitis was then studied. Mammary secretions were collected from a cow dried for a month. Whey was prepared by acid precipitation at pH 4.6 and centrifugation at Materials and Methods 25 000 g for 40 min. The whey was dialysed against 0.05 M NaCl in 5 mM veronal-HCI (pH Herd and experimental design 7.4) and applied to a 1.0 x 14 cm column of Heparin-Sepharose CL-6B (Pharmacia Fine Che- Forty-two Holstein and Fresian-Holstein micals, Uppsala, Sweden) equilibrated with cross-bred cows of our experimental herd were 0.05 M NaCl in the veronal buffer, according to used for the Quarter foremilk study. samples B16ckberg (1980), except that the elution step were obtained at three week intervals. routinely was modified as follows : the column was Data are from milk and blood collected samples washed with 50 ml of the same buffer. The at 30, 150 and 270 of lactation. Several days eluted proteins were discarded. The column was samples were not available for analysis because then eluted with 0.6 M NaCl in the veronal buffer. of blind quarters or losses. culling, The red peak emerging from the column was collected and dialysed against 0.2 M sodium of milk and blood samples Processing acetate buffer. This material was then applied to All samples were collected at the evening a 2.5 x 20 cm column of carboxymethyl cellulose milking. Milk samples were prepared by centrifu- (CM 52, Whatman Ltd., Springfield, England). The gation of whole milk at 1 500 g for 20 min to column was eluted with a linear gradient consis- remove cells and fat. Casein was precipitated by ting of 500 ml of 0.2 M sodium acetate as addition of rennet and incubation at 37 °C for starting buffer and 500 ml of 0.8 M sodium one hour. Samples were then centrifuged twice acetate as the limit solvent. The red peak was at 2 500 g for 30 min. collected, concentrated using a Diaflo PM 10 in an Blood samples were obtained by tail vein membrane Amicon stirred ultrafiltration cell puncture. They were allowed to clot at room (Amicon, Lexington, Ma, USA), dialysed against temperature and sera were separated by centri- 0.01 M ammonium bicarbonate, and freeze dried. fugation at 1 000 g for 20 min. Serum and whey Confirmation that the protein preparation was samples were stored frozen ( - 20 °C) until need- lactoferrin was shown by immunoelectrophore- ed. sis against a rabbit antiserum raised against bovine lactoferrin kindly supplied by A.W. Hill Protein quantitation (ARC Institute for Research on Animal Diseases, Transferrin and lactoferrin concentrations in Compton, Newbury, England). The preparation serum and whey were determined by the radial (50 mg/ml) gave only one line in precipiting immunodiffusion procedure of Mancini et al. immunoelectrophoresis against rabit anti-bovine (1965). Every whey sample was tested in dry secretion and no line against rabbit anti- duplicate and the mean value was used in bovine serum. determining concentration. When duplicate values differed by more than 15 %, the sample was tested again. Preparation of transferrin One volume of bovine serum was diluted with three volumes of 0.005 M Tris-HCI buffer pH 8.8 Results and then precipitated with four volumes of rivanol (6.9 diamino-2-ethoxy-acridine lactate, concentrations of lactoferrin and Sigma Chemical Company, St-Louis, Mo, USA) at Average transferrin from all of the 376 of milk 0.6 % (w/v) at 4 °C. After elimination of the samples from non-infected were precipitate by centrifugation at 13 000 for quarters respectively and con- 45 min, NaCI was added to a final concentration 0.080 mg/ml 0.030 mg/ml. Average centration of transferrin in serum (122 of 5 % (w/v) to precipitate rivanol. The mixture samples) was This concentration was agitated overnight at 4 °C then centrifuged 4.63 mg/ml. average varied little lactation In and dialysed against phosphate buffered saline. during (table 1). fact, individual variations this time were consi- (The pH was brought to 6.5 by adding 1 M during acetate-acetic acid buffer pH 6.3). lmmunoglo- derable, often with concentrations doubling, without any trend, which bulins were precipitated with 50 % final satu- though systematic these fluctuations did rated ammonium sulphate. After centrifugation explains why not influence the average levels. The extreme values (table 1) the supernatant was dialysed against 0.02 M illustrate the range of these fluctuations.
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