Separation of Lactoferrin-a and -b from Bovine Colostrum

Abstract

Bovine lactoferrin was separated into lactoferrin-a and lactoferrin-b from bovine colostrum. Lactoferrin-a was eluted at 0.38 M NaCl and lactoferrin-b was eluted at 0.43 M NaCl by carboxymethyl cation-exchange chromatography at pH 7.7, 0.05 M phosphate buffer. The molecular weights were estimated at 84,000 for lactoferrin-a and 80,000 for lactoferrin-b. Lactoferrin-a contents were 258.0 mg/L and lactoferrin-b contents were 524.3 mg/L of colostrum for cow 19. From colostrum to normal milk, total lactoferrin was from 17.1 to 129.4 mg/L during the normal lactational period; however, lactoferrin did not separate clearly into lactoferrin-a and lactoferrin-b. The lactoferrin-a measured from six cows was 258.0, 114.0, 112.8, 64.0, 59.7, and 22.4 mg/ L and the lactoferrin-b 524.3, 331.8, 184.7, 170.7, 129.3, and 44.0 mg/L, respectively. The average was 105.2 mg (31.3%) for lactoferrin-a and 230.8 mg (68.7%) for lactoferrin-b.

Immunoregulatory role of lactoferrin-lipopolysaccharide interactions

“…Interestingly, the concentration of bLf-a, which has a higher molecular mass than bLf-b, in colostrum is greater than in normal milk. As bLf-a was found to exhibit a stronger bactericidal activity against Escherichia coli than bLf-b, it was suggested that bLf-a may play an important healthy role in colostrum drinking calves (Yoshida et al 2000). Lastly, the presence of mannose-type glycans in bLf molecule has been described to be responsible for its capacity to induce mannose receptor-dependent delayed type hypersensitivity (DTH) response to ovalbumin (OVA) in mice Zimecki et al 2002).…”

Use of Wisteria floribunda agglutinin affinity chromatography in the structural analysis of the bovine lactoferrin N-linked glycosylation

“…Human LF consists of 691 amino acids and contains 3 potential glycosylation sites at Asn138, Asn479, and Asn624; Asn138 and Asn479 are occupied with complex-type N-glycans, whereas Asn624 is usually unoccupied [25,26]. Bovine LF consists of 689 amino acids and has 5 potential glycosylation sites at Asn233, Asn288, Asn368, Asn476, and Asn545; Asn233, Asn368, Asn467, and Asn545 are always occupied, and Asn288 is occupied for about 30% [18,19,27].…”

Proteinograma da secreção láctea de cabras

“…Essas observações estão de acordo com os estudos anteriores que referiram à maior concentração de lactoferrina no colostro e diminuição na sua concentração com o evoluir dos dias de lactação para vacas (SANCHEZ et al, 1988;TSUJI et al, 1990;HENG, 1999;YOSHIDA et al, 2000;BAROZA, 2007;HISS;MEYER;SAUERWEIN, 2008;ROCHA et al, 2009) e cabras (SANCHEZ et al, 1988;TSUJI et al, 1990;HENG, 1999;YOSHIDA et al, 2000; Resultados e discussão Raimondo, R. F. S. HISS;MEYER;SAUERWEIN, 2008;ROCHA et al, 2009). …”

“…Na literatura compulsada há discrepância nos valores de lactoferrina encontrados no colostro possivelmente devido as diferentes técnicas utilizadas (TSUJI et al, 1990;YOSHIDA et al, 2000). No estudo das proteínas do colostro de cabras através da técnica de eletroforese SDS-PAGE, Baroza (2007) observou diminuição da concentração de lactoferrina durante o 1º mês de lactação, pois os valores máximos obtidos no dia do parto iguais a 396 ± 78 mg/dL diminuíram abruptamente no 1º dia de lactação (98,3…”

“…Entretanto existe discrepância nos teores lácteos de lactoferrina no colostro possivelmente devido às diferentes técnicas utilizadas (TSUJI et al, 1990;YOSHIDA et al, 2000) ou decorrentes a influência da espécie, pois segundo Masson e Heremans (1971) o colostro bovino contém concentrações menores de lactoferrina quando comparado com outras espécies.…”