Separation of the submicelles from micellar casein by high performance gel chromatography on a TSK-GEL G4000SW column

Ono, Tomotada; Odagiri, Satoshi; Takagi, Toshio

doi:10.1017/s0022029900032507

Cited by 17 publications

(15 citation statements)

References 18 publications

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“…3. These first peaks (I) were F2 subunit which had been reported previously to consist of <z s -casein and /c-casein (Ono et al 1983). The peak corresponding to F2 subunit was not detected for equine casein, which contained no K-casein.…”

Section: Oel Chromatography Of Micellar Caseinmentioning

confidence: 61%

“…The Fl peak containing /c-casein polymer had been detected previously by u.v. monitoring (Ono et al 1983). However, Fl was hardly observed, ahead of F2 peak, by refractometry.…”

Section: Oel Chromatography Of Micellar Caseinmentioning

confidence: 93%

“…Similar casein particles have also been found in dialysed bovine milk (Schmidt & Buchheim, 1970;Heth & Swaisgood, 1982). In spite of their similar size, the casein particles in the bovine and caprine dialysed milks could be separated into four fractions (F1-F4) by high-performance gel chromatography (HPGC) on TSK-G4000SW and Sephacryl S-400 columns respectively (Ono et al 1983;Ono & Creamer, 1986). Although the molecular weights and compositions of the major submicellar fractions (F2 and F3) of bovine casein have been investigated (Ono & Takagi, 1986), those of caprine, ovine and equine casein are not known, and the subunit components of ovine and equine casein micelles have not been separated.…”

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confidence: 99%

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Subunit components of casein micelles from bovine, ovine, caprine and equine milks

Ono

Kohno

Odagiri

et al. 1989

Journal of Dairy Research

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Subunit components of ovine, caprine and equine casein micelles were separated by gel chromatography using a TSK-G4000SW high-performance column and the subunit components of the fractions analysed and compared with bovine casein. Molecular weights of the casein complexes were determined by the combined use of high-performance gel chromatography and low-angle laser light scattering. The caprine and ovine caseins were separated into three peaks (F2, F3 and F4) which were similar to those of bovine casein with respect to composition and molecular weight (500, 100 and 23 K). These F2, F3 and F4 peaks consisted mainly of a s -and /c-casein, a s -and /?-casein and /?-casein respectively. The equine casein was separated into two components corresponding to F3 and F4 of bovine casein. These F3 and F4 peaks consisted mainly of a s -and /?-casein and /?-casein respectively. The molecular weight of equine F3 (850 K) was different from that of the other three species. The contents of F2 and F4 in these caseins were dependent on the contents of /e-casein and /?-casein respectively.

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Section: Oel Chromatography Of Micellar Caseinmentioning

confidence: 61%

“…The Fl peak containing /c-casein polymer had been detected previously by u.v. monitoring (Ono et al 1983). However, Fl was hardly observed, ahead of F2 peak, by refractometry.…”

Section: Oel Chromatography Of Micellar Caseinmentioning

confidence: 93%

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confidence: 99%

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Subunit components of casein micelles from bovine, ovine, caprine and equine milks

Ono

Kohno

Odagiri

et al. 1989

Journal of Dairy Research

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“…Two different types of submicelles were observed by high-performance gel chromatography (Ono, Odagiri, & Takagi, 1983); they vary in composition, size and position in the micelle. The internal ones are smaller (10 nm in diameter with a molecular weight of 110,000-190,000) than the outer (20 nm, 490,000710,000), which contain k-caseins (Ono & Takagi, 1986;Ono & Obata, 1989).…”

Section: Introductionmentioning

confidence: 99%

Heat induced aggregation and gelation of casein submicelles

Panouillé

Nicolai

Durand

2004

International Dairy Journal

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“…In that proposed by Schmidt (1982) submicelles were held together by CCP. Submicelles are heterogeneous in their composition and Ono et al (1983) separated submicelles by high-performance gel chromatography. From their findings it was suggested that several types of submicelles exist, namely complexes of a sl -with /c-cascin, and of a s]with /?-casein, and polymers of a sl -and /?-casein.…”

Section: Resultsmentioning

confidence: 99%

Incorporation of individual casein constituents into casein aggregates cross-linked by colloidal calcium phosphate in artificial casein micelles

Aoki¹

1989

Journal of Dairy Research

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Artificial casein micelles were prepared at a casein concentration of 2-5% with 10-40 niM-Ca, 12-27 mM-phosphate and 10 mM-citrate and cross-linking of casein by colloidal Ca phosphate (CCP) was examined. No casein aggregates crosslinked by CCP were formed at 10 mM-Ca, 12 mM-phosphate and 10 mM-citrate, which are the approximate concentrations found in the soluble phase of bovine milk. Although the amounts of casein aggregates cross-linked by CCP and of colloidal inorganic phosphate increased with increasing Ca and phosphate concentrations, the effect was not uniform. The incorporation rates of individual casein constituents into casein aggregates cross-linked by CCP were in the order a s2 -> a sl -> /?-casein. This was the reverse of the order of dissociation rates during dialysis of casein aggregates cross-linked by CCP reported previously.Bovine casein micelles are roughly spherical colloidal particles of 20-600 nm diam., which are heterogeneous in constitution (Schmidt, 1982). They are composed of 93 % casein and 7 % inorganic constituents. The main inorganic constituent of casein micelles is colloidal Ca phosphate (CCP). Direct experimental evidence for this has been obtained by Aoki et al. (1986), who isolated casein aggregates cross-linked by CCP from bovine casein micelles by high-performance gel chromatography on a TSK-GEL G4000SW column in the presence of 6 M-urea. It has also been shown that caseins are cross-linked through their ester phosphate groups by CCP (Aoki et al. 19876).Bovine caseins are synthesized in the mammary gland and micelle formation occurs in the Golgi vesicles. It is assumed that casein submicelles are aggregated into micelles by CCP formed by transformation of Ca, phosphate and other inorganic constituents from cytosol to the Golgi vesicles (Schmidt, 1982;Holt, 1985). However, the formation of cross-linkages between casein molecules and CCP in the bioassembly of casein micelles has not yet been elucidated sufficiently.In a previous study (Aoki et al. 1988) we examined the dissociation during dialysis of casein aggregates cross-linked by CCP in bovine micelles, and elucidated that the dissociation rates of individual casein constituents were in the order /?-> a sl -> a s2 -casein. The higher the ester phosphate content, the slower was the dissociation rate of individual casein constituents. These facts suggested that the strength of the bonding between casein molecules and CCP depended on the ester phosphate content.

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Separation of the submicelles from micellar casein by high performance gel chromatography on a TSK-GEL G4000SW column

Cited by 17 publications

References 18 publications

Subunit components of casein micelles from bovine, ovine, caprine and equine milks

Subunit components of casein micelles from bovine, ovine, caprine and equine milks

Heat induced aggregation and gelation of casein submicelles

Incorporation of individual casein constituents into casein aggregates cross-linked by colloidal calcium phosphate in artificial casein micelles

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