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Neutrophil gelatinase-associated lipocalin : a protein involved in immune defense against microbial pathogens /Goetz, David Henry. January 2002 (has links)
Thesis (Ph. D.)--University of Washington, 2002. / Vita. Includes bibliographical references (leaves 62-74).
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Study of sPDZD2 function using in vitro and in vivo approachesTam, Siu-man, Tammy., 談少雯. January 2004 (has links)
published_or_final_version / abstract / toc / Biochemistry / Master / Master of Philosophy
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MIR, a novel ERM-like protein in the nervous system /Olsson, Per-Anders, January 1900 (has links)
Diss. (sammanfattning) Uppsala : Univ., 2001. / Härtill 3 uppsatser.
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The cell cycle regulators p15, p16, p18 and p19 : functions and regulation during normal cell cycle and in multistep carcinogenesis /Thullberg, Minna, January 1900 (has links)
Diss. (sammanfattning) Stockholm : Karol. inst. / Härtill 6 uppsatser.
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Horse plasma vitamin D-binding protein : isolation and structural investigationRobinson, Robert Charles January 1990 (has links)
Vitamin D-binding protein (DBP) is an abundant serum protein, secreted by the liver, which transports vitamin D sterols and is part of an actin scavenging system. In this study, DBP was isolated from horse plasma in a highly reproducible, four step procedure: Affi-gel Blue affinity chromatography, gel filtration, hydroxy1apatite chromatography and anion exchange HPLC. 6-7 mg of DBP were obtained from 80 ml of plasma with a yield of 21-25%.
The secondary structure of DBP was calculated from circular dichroism measurements to be 39% α-helix, 42% β-sheet and 19% random coil. A molecular mass of 53,000 ± 3,000 daltons was calculated from electrophoretic gels. Circular dichroism and fluorescence studies revealed that the disulphide bonds of DBP contribute substantial structural stabilization to the molecule with respect to thermal denaturation.
Finally, acrylodan-labeled DBP was prepared. The fluorescence of this adduct was sensitive to the binding of actin and to the presence of dithiothreitol. / Science, Faculty of / Chemistry, Department of / Graduate
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Design and synthesis of artificial glycopolypeptides as mediators of biologically relevant binding eventsPolizzotti, Brian D. January 2007 (has links)
Thesis (Ph.D.)--University of Delaware, 2006. / Principal faculty advisor: Kristi L. Kiick, Dept. of Materials Science & Engineering. Includes bibliographical references.
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Expression, purification and preliminary x-ray crystallographic studies of two nucleotide binding proteinsLaw, Wing-lun., 羅永倫. January 2011 (has links)
published_or_final_version / Physiology / Master / Master of Philosophy
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Drug transporters and blood-testis barrier dynamicsSu, Linlin., 苏琳琳. January 2011 (has links)
published_or_final_version / Biological Sciences / Doctoral / Doctor of Philosophy
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A study of p53-binding protein 1 in sperm functionYu, Oi-yan, 余靄恩 January 2013 (has links)
Spermatozoa experience a series of physiological alternation upon traveling from the testis to the epididymis in order to acquire motility and capacity necessary to recognize and to fuse with an oocyte. Further maturation and modification of the spermatozoa occur along the journey in the female reproductive tract in a process known as capacitation. p53 protein is a well-known transcription factor involved in guarding of genome integrity by triggering cell cycle arrest and cell death upon DNA damage. p53-binding protein 1 (53BP-1) binds to p53 and enhances p53-mediated transcriptional activity. It has been reported that human spermatozoa produce 53BP-1 for DNA repair in response to oxidative stress. 53BP-1 is expressed in pre-implantation embryos. The current study aimed to identify the expression and subcellular location of 53BP-1 proteins in mouse spermatozoa by immunofluorescence staining. Increased expression of 53BP-1 proteins was found in the swim-up and capacitated mouse spermatozoa. The immunoreactivity was localized to the sperm head and midpiece, suggesting possible roles of 53BP-1 in sperm function. It was also found that mouse oocytes and 1-cell embryo also expressed 53BP-1. The potential function of 53BP-1 in early embryo development was also investigated using 53BP-1 antibody neutralized sperm in in-vitro fertilization. There was no significant difference between the development rate of embryos fertilized with spermatozoa transduced with anti-53BP-1 antibody and those that transduced with the control goat IgG. Further studies are needed to investigate the role of sperm 53BP-1 at later stage of embryo development and implantation. / published_or_final_version / Obstetrics and Gynaecology / Master / Master of Medical Sciences
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Characterization of TM4 of NRAMP1: implication for FEII transportKwan, Miu-fan., 關妙芬. January 2003 (has links)
published_or_final_version / abstract / toc / Chemistry / Master / Master of Philosophy
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