Milk Proteins

McKenzie, H.A.

doi:10.1016/s0065-3233(08)60041-8

Cited by 157 publications

(51 citation statements)

References 406 publications

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“…For example, a-casein and p-casein can also be precipitated with calcium but they contain 1.0% and 0.6% phosphorus, respectively. T h e caseins also are larger proteins [19]. Although by definition a glycoprotein, CaPP is very different from the epithelial mucins, which have a very high molecular weight, contain many carbohydrate side chains composed of hexosamine, sialic acid, and fucose, as well as galactose (hexose) residues, and give the mucus secretions their characteristic viscous properties [26].…”

Section: Discussionmentioning

confidence: 99%

“…Additional samples of CaPP were purified from 30-100 ml of saliva, collected from six patients with CF (ages [14][15][16][17][18][19][20][21][22][23][24][25][26] and six normal subjects (ages [18][19][20][21][22][23][24][25][26][27][28][29][30]. A modified Schneyer collecting technique [lo, 241 and stimulation with sour lemon drops were used for all collections.…”

Section: Saliva Collectionsmentioning

confidence: 99%

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Purification and Properties of the Calcium-precipitable Protein in Submaxillary Saliva of Normal and Cystic Fibrosis Subjects

1974

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ExtractA calcium-precipitable protein (CaPP), previously shown to cause turbidity of submaxillary saliva (SMS) in patients with cystic fibrosis (CF), was purified from normal and CF-SMS by (NH4) 2 S 0 4 precipitation, gel filtration, and preparative polyacrylamide gel electrophoresis. This protein has a molecular weight of 12,000. I t contains large numbers of serine, glycine, and glutamic acid residues, 0.85y0 phosphorus as phosphate monoester, and small amounts of carbohydrate. Precipitation (aggregation) of purified CaPP occurs at basic pH values in the presence of ionic calcium and is enhanced by increasing calcium concentration, CaPP concentration, or pH. Aggregated CaPP binds calcium in molar quantities equal to the number of phosphate prosthetic groups. Alkaline phosphatase removes all phosphate from CaPP and eliminates calcium-induced precipitation. Studies of CaPP from CF saliva have demonstrated no electrophoretic or compositional differences from normal CaPP. Higher than normal pH values or elevated CaPP concentrations are not present in SMS of patients with CF and do not contribute to the formation of turbid SMS.

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Section: Discussionmentioning

confidence: 99%

Section: Saliva Collectionsmentioning

confidence: 99%

Purification and Properties of the Calcium-precipitable Protein in Submaxillary Saliva of Normal and Cystic Fibrosis Subjects

1974

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“…The extent of lysine modification was determined by the method of Habeeb (30) with trinitrobenzenesulfonic acid as the difference in lysyl residues of modified and unmodified protein preparations. Molar ratios were calculated assuming a total molecular weight of 500,000 for protein of LDL (31), 66,210 for half-cystyl bovine plasma albumin (32), 68,900 for maleyl-albumin (15), and 27,400 for bovine a-casein (33). Chemical derivatization of LDL by malondialdehyde typically resulted in modification of 38-48% of the lysyl residues of the apolipoprotein B polypeptides; maleylation, acetylation, and reductive methylation of albumin resulted in modification of >94% ofthe peptidyl lysines.…”

Section: Introductionmentioning

confidence: 99%

Two distinct receptors account for recognition of maleyl-albumin in human monocytes during differentiation in vitro.

Rasmussen¹,

Olch²,

Fogelman³

1986

J. Clin. Invest.

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A comparison of the receptor-mediated interaction of malondialdehyde-low density lipoprotein and maleyl-albumin has been examined in human monocytes during differentiation in vitro. The recognition of both ligands by the scavenger receptor of these cells has been confirmed. We now report that human monocytes express a second cellular surface receptor for maleylalbumin that is distinct from the scavenger receptor. The activity of the maleyl-albumin receptor, determined by both binding and lysosomal hydrolytic assays, substantially exceeds that of the scavenger receptor in freshly isolated monocytes. A dramatic and rapid decline in the activity of the maleyl-albumin receptor occurs within 72 to 96 h during differentiation in vitro. At day 7, while only 5-10% of the original activity of the maleyl-albumin receptor remains, it is similar to that of the maximally expressed scavenger receptor. Both the binding and hydrolysis of ligand mediated by the maleyl-albumin receptor are specifically inhibited by a-casein and alkaline-treated albumin; neither of these proteins is recognized by the scavenger receptor.The occurrence of the exceptionally active maleyl-albumin receptor on freshly isolated human monocytes suggests that it participates in processes necessary to the function of the cells that diminish in importance after differentiation of the monocytes into macrophages in vitro. Furthermore, while maleyl-albumin is a useful adjunct to studies of cellular events mediated by the scavenger receptor, the presence of a second receptor for maleylalbumin must be taken into account as a potential contributing and complicating event.

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“…Whole casein was either 'Hammarsten casein' from Merck, Darmstadt, Germany, or it was prepared by acid precipitation at 30°C (McKenzie, 1967) from the skimmed milk of a single cow of Bavarian breed. a,,-and aC2-caseins were prepared from acid casein as described by Mercier et al (1968) and Brignon et al (1976) respectively.…”

Section: Methodsmentioning

confidence: 99%

Phosphorylation of threonine and serine residues of native and partially dephosphorylated caseins by a rat liver cyclic AMP-insensitive protein kinase

Deana¹,

Meggio²,

Pinna³

1979

Biochemical Journal

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The preferential phosphorylation of threonine residues of native casein fractions by a rat liver cyclic AMP-independent protein kinase (EC 2.7.1.37) is abolished by preliminary limited dephosphorylation of the substrates, which promotes a fall in the phosphothreonine/phosphoserine ratios from values higher than I to much less than 0.1. This finding and the identification of the threonine residues phosphorylated support the view that the liver protein kinase affects threonine residues only when suitable serine residues, which fulfil the stiuctural requirements for attack by the enzyme but which are not yet phosphorylated, are not available.

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Milk Proteins

Cited by 157 publications

References 406 publications

Purification and Properties of the Calcium-precipitable Protein in Submaxillary Saliva of Normal and Cystic Fibrosis Subjects

Purification and Properties of the Calcium-precipitable Protein in Submaxillary Saliva of Normal and Cystic Fibrosis Subjects

Two distinct receptors account for recognition of maleyl-albumin in human monocytes during differentiation in vitro.

Phosphorylation of threonine and serine residues of native and partially dephosphorylated caseins by a rat liver cyclic AMP-insensitive protein kinase

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