The Disulfide Bonds of Bovine α-Lactalbumin
نویسندگان
چکیده
منابع مشابه
Lipid binding specificity of bovine α-lactalbumin: a multidimensional approach.
Many soluble proteins are known to interact with membranes in partially disordered states, and the mechanism and relevance of such interactions in cellular processes are beginning to be understood. Bovine α-lactalbumin (BLA) represents an excellent prototype for monitoring membrane interaction due to its conformational plasticity. In this work, we comprehensively monitored the interaction of ap...
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α-Lactalbumin is the second major protein in bovine milk (2-5% of the total protein in bovine milk). The human variant has several physiologic functions in the neonatal period. In the mammary gland, it participates in lactose synthesis and facilitates milk production and secretion. α-Lactalbumin binds divalent cations (Ca Zn) and may facilitate the absorption of essential minerals. Also, it pro...
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Bovine α-lactalbumin is known to be present in molten globule form in its apo-state (i.e., Ca depleted state). In this preliminary study, heat-induced conformational changes were analyzed using the fluorescence spectroscopy at very low pH in the absence and the presence of calcium ions. The heat treatment caused the decrease of intrinsic fluorescence, evidencing the increase of intramolecular q...
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The completed amino-acid sequence of bovine neurophysin-II, a major neurohypophyseal hormone-binding protein in the hypothalamo-neurohypophyseal complex of cows, set the stage for the localization of the disulfide bonds of this sulfur-rich molecule. Neurophysin-II was digested with subtilisin or a pepsin-trypsin mixture. The resulting peptides were subjected to first-dimensional electrophoresis...
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The inter- and intrasubunit disulfide bridges for the 11 S form of acetylcholinesterase isolated from Torpedo californica have been identified. Localized within the basal lamina of the synapse, the dimensionally asymmetric forms of acetylcholinesterase contain either two (13 S) or three (17 S) sets of catalytic subunits linked to collagenous and noncollagenous structural subunits. Limited prote...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)63828-7