Lactose synthetase activity of α-lactalbumins from several species

Ley, Janice; Jenness, Robert

doi:10.1016/0003-9861(70)90370-x

Cited by 41 publications

(9 citation statements)

References 7 publications

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“…On the basis of kinetic studies (Brodbeck & Ebner, 1966;Morrison & Ebner, 1971a,b,c), it has been predicted that the amount of lactose in milk should be proportional to the a-lactalbumin content (Ebner & McKenzie, 1972). This reasoning was supported by the results of Ley & Jenness (1970), showing a significant positive correlation between the concentration of these two components in the milk of six selected species.…”

supporting

confidence: 58%

α-Lactalbumin and lactose concentrations in rat milk during lactation

Nicholas¹,

Hartmann²,

McDonald³

1981

Biochemical Journal

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Homogeneous rat alpha-lactalbumin was prepared from whey by chromatography on DEAE-Sephadex A-50 and Ultrogel AcA 44. Two biologically active forms of alpha-lactalbumin were apparent after ion-exchange chromatography, but on gel filtration the combined forms were eluted as a single peak with a molecular weight of approx. 33000. The molecular weight when determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis was 15100. Antiserum to alpha-lactalbumin was prepared from rabbits, and single radial immunodiffusion was used to measure the concentration of alpha-lactalbumin in milk expressed from rats during lactation and for 2 days after the cessation of lactation. A significant positive correlation (r = + 0.89) between the concentrations of alpha-lactalbumin and lactose was obtained for the first 20 days of lactation. This is consistent with the suggestion that alpha-lactalbumin may control the concentration of lactose in milk. However, a significant negative correlation (r = -0.91) between the concentration of alpha-lactalbumin and lactose was obtained for 2 days after the cessation of lactation on day 20.

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supporting

confidence: 58%

α-Lactalbumin and lactose concentrations in rat milk during lactation

Nicholas¹,

Hartmann²,

McDonald³

1981

Biochemical Journal

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“…a-Lactalbumin and lactoferrin accounted for about 30 and 18% of the total protein content, respective ly. Varying amounts of a-lactalbumin have been reported in human milk, ranging from 0.28 to 0.48 g/dl [7], Forsum [8] reported that a-lactalbumin. as determined by electroim munoassay in the milk provided by 1 moth er, varies from 0.29 to 0.48 g/dl.…”

Section: Discussionmentioning

confidence: 99%

“…Human milk con tains P-and K-caseins but does not contain a-caseins [3,4], a-Lactalbumin, lactoferrin, serum albumin, and other minor fractions such as lysozyme and immunoglobulins are also present [3][4][5][6], In contrast to bovine milk, human milk does not contain p-lactoglobulin [2], a-Lactalbumin and lactoferrin are re ported to decrease from human colostrum to mature milk, but contradictory values have been reported for both proteins [5][6][7][8]. Lyso zyme increases and immunoglobulins de crease during the same period [9].…”

mentioning

confidence: 99%

Changes in the Protein Fractions of Human Milk during Lactation

et al. 1986

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The changes in the absolute and relative contents of α- and ĸ-caseins, lactoferrin, α-lactalbumin, serum albumin and lysozyme in human milk have been studied through the period of lactation. Protein fractions of 209 samples were analyzed by a discontinuous poly-acrylamide gel electrophoresis method, β- and ĸ -caseins decreased from colostrum to mature milk although their relative percentages remained constant. They accounted for 12–15 and 9–13% of the total protein in human milk, respectively. Lactoferrin decreased in absolute and relative amounts with advancing lactation. This protein represented 32–19% of the human milk proteins. α-Lactalbumin slightly decreased from colostrum to transitional milk but there was an increase in mature milk by 16–30 days. The percentages of this protein in colostrum and mature milk were approximately 23 and 30%, respectively. Serum albumin also decreased with advancing lactation, but the differences between transitional and mature milk were not statistically significant. Lysozyme increased from colostrum to mature milk both in relative and absolute amounts. Colostrum contained about 262 µg/ml, and mature milk 1,246 µg/ml, representing 1.5 and 12.1% of total milk proteins.

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“…General references [67,68]. Specific references for milk composition are: bovine [4,67,69], mouse and rat [70][71][72][73][74], human [75], pig [55], sheep and goat [76], and Kangaroo [77][78][79] The application of functional genomics and bioinformatics allows for a thorough exploration of the biological complexity of organisms' tissues [34]. Together, these approaches form part of the systems biology framework, i.e., a way to systematically study the complex interactions in biological systems using a method of integration instead of reduction.…”

Section: Transcriptomics: a Novel Approach To Study Biologymentioning

confidence: 99%