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Titlebook: Lactoferrin; Interactions and Bio T. William Hutchens,Bo Lönnerdal Book 1997 Humana Press Inc. 1997 Expression.Leishmania.gene expression.i

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书目名称Lactoferrin
副标题Interactions and Bio
编辑T. William Hutchens,Bo Lönnerdal
视频video
丛书名称Experimental Biology and Medicine
图书封面Titlebook: Lactoferrin; Interactions and Bio T. William Hutchens,Bo Lönnerdal Book 1997 Humana Press Inc. 1997 Expression.Leishmania.gene expression.i
描述The number of investigators focusing their attention on lactoferrin has increased dramatically in recent years. Lactoferrin is a protein with more than one known structure and a number of proposed biological functions, including several with important regulatory consequences. In many ways it has been an easy pro­ tein to investigate; however, there have been difficulties under­ standing specific structure / function relationships, particularly as it functions in vivo. Research funding dedicated to this protein has previously been limited, but is now increasing. As lactoferrin begins to emerge formally as a protein of significance to the medi­ and industry, it is more important than ever to coor­ cal profession dinate and integrate research efforts whenever possible and to share the results of these efforts within the expanding array of medical and scientific diSciplines involved. It was our intention to provide a forum to summarize and disseminate the most recent advances in this field. Included in Lactoferrin: Interactions and Biological Functions are selected presentations representing the many disciplines involved in defining lactoferrin function in terms of its known structural
出版日期Book 1997
关键词Expression; Leishmania; gene expression; influence; metabolism; mutagenesis; protein; regulation; transcript
版次1
doihttps://doi.org/10.1007/978-1-4612-3956-7
isbn_softcover978-1-4612-8439-0
isbn_ebook978-1-4612-3956-7
copyrightHumana Press Inc. 1997
The information of publication is updating

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Mutagenesis of Human Lactoferrin and Expression in Baby Hamster Kidney Cells (BHK) cells (Stowell et al, 1991; Day et al., 1992). The properties of the full-length recombinant protein produced in this system were virtually indistinguishable from those of the native protein isolated from human milk, except for an increased resistance of a minor fraction of the protein to deg
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Structural Determination of Two N-Linked Glycans Isolated from Recombinant Human Lactoferrin Expressscribed by Stowell et al. (1991). Two N-linked glycans from purified recombinant lactoferrin were released by hydrazinolysis and analyzed by 400-MHz .H-NMR spectroscopy. The identified structures corresponded to .-acetyllactosaminic biantennary glycans and were α-2,3-disialylated forms (80%) or α-2,
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