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Journal ArticleDOI

Enzymic assay for galactosyl transferase activity of lactose synthetase and α-lactalbumin in purified and crude systems☆

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TLDR
The enzymic assay for the A protein of lactose synthetase (galactosyl transferase) was carefully evaluated using bovine α-lactalbumin to assay for purified bovines A protein and the Aprotein in rat mammary homogenates.
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This article is published in Analytical Biochemistry.The article was published on 1970-07-01. It has received 156 citations till now. The article focuses on the topics: Lactose synthase & Alpha-lactalbumin.

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Citations
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Journal ArticleDOI

Carbohydrate mimetics-based glycosyltransferase inhibitors.

TL;DR: The purpose of this account is to foster a synergy between the two expanding research areas of glycomimetics and glycosyltransferases.
Journal ArticleDOI

The use of hydrophobic synthetic glycosides as acceptors in glycosyltransferase assays

TL;DR: A general method is described for the assay of glycosyltransferase activity, which makes use of synthetic glycoside acceptors attached to hydrophobic aglycones, which can be rapidly separated from interfering radioactivity by adsorption on to reverse-phase C-18 cartridges.
Book ChapterDOI

Lysozyme and alpha-lactalbumin: structure, function, and interrelationships.

TL;DR: This chapter considers both the structure and function of α-lactalbumin and lysozyme in relation to each other, and also the potential significance of the studies in health and the pathology of disease, such as cancer.
Journal ArticleDOI

Galactosyltransferase Acceptor Specificity of the Lactose Synthetase A Protein

TL;DR: The biosynthesis of lactose and the formulation of the Gal-β-1,4-GlcNAc linkage in the carbohydrate side chain of glycoproteins are compatible and are carried out by the same galactosyltransferase.
Journal ArticleDOI

Growth control and differentiation in mammary epithelial cells.

TL;DR: Complete or partial sequencing of several milk protein genes and comparative analysis have led to identification of a sequence of high homology and conservation in the 5' flanking region that is likely to be involved in the regulation of milk protein gene expression.
References
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Journal ArticleDOI

The Isolation and Identification of the B Protein of Lactose Synthetase as α-Lactalbumin

TL;DR: In this article, the B protein α-lactalbumin was identified as a natural occurring subunit of lactose synthetase based on substitution in the enzymic rate assays, spectra, immunological titrations, amino acid composition, mobility on starch gel electrophoresis, molecular weight, and cochromatography on diethylaminoethyl cellulose and Sephadex G-100.
Journal ArticleDOI

Comparison of the Amino Acid Sequence of Bovine α-Lactalbumin and Hens Egg White Lysozyme

TL;DR: It is proposed that an ancestral gene which controlled the sequence of a lysozyme-like enzyme duplicated, and the duplicate genes evolved independently giving rise to the genes for α-lactalbumin and the lysozymes.
Journal ArticleDOI

Resolution of a Soluble Lactose Synthetase into Two Protein Components and Solubilization of Microsomal Lactose Synthetase

TL;DR: The partial purification and resolution of the soluble lactose synthetase into two protein components, A and B, which individually do not exhibit any catalytic activity is discussed.
Journal ArticleDOI

The Hormonal Control of Lactose Synthetase in the Developing Mouse Mammary Gland

TL;DR: The asynchronous expression of the A and B proteins may represent a unique type of hormonal control of a biosynthetic pathway, and appears to reflect the specific functional requirements of the mammary gland during development and lactation.
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