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Proteomic studies of human breast ca...

Hamler, Rick L.

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Proteomic studies of human breast cancer cell lines using multidimensional separation techniques and time-of-flight mass spectrometry.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Proteomic studies of human breast cancer cell lines using multidimensional separation techniques and time-of-flight mass spectrometry./
Author:	Hamler, Rick L.
Description:	144 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0688.
Contained By:	Dissertation Abstracts International64-02B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3079455

Proteomic studies of human breast cancer cell lines using multidimensional separation techniques and time-of-flight mass spectrometry.
Hamler, Rick L.

Proteomic studies of human breast cancer cell lines using multidimensional separation techniques and time-of-flight mass spectrometry. - 144 p.

Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0688.

Thesis (Ph.D.)--University of Michigan, 2003.

In this work, a two-dimensional liquid-phase separation technique coupled with time-of-flight mass spectrometry (TOF-MS) is presented for proteomic studies of human breast cancer. Preparative liquid isoelectric focusing was performed as the first dimension, and nonporous silica reverse-phase high-performance liquid chromatography (NPS RP-HPLC) as the second dimension. NPS RP-HPLC was directly coupled with electrospray ionization (ESI) TOF-MS to obtain accurate intact protein molecular weights. Furthermore, mass fingerprinting and tandem mass spectrometry were performed on tryptic digests of proteins using matrix-assisted laser desorption ionization (MALDI) TOF-MS.Subjects--Topical Terms:

586156
Chemistry, Analytical.

Proteomic studies of human breast cancer cell lines using multidimensional separation techniques and time-of-flight mass spectrometry.
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035 $a (UnM)AAI3079455
035 $a AAI3079455
040 $a UnM $c UnM
100 1 $a Hamler, Rick L. $3 1945906
245 1 0 $a Proteomic studies of human breast cancer cell lines using multidimensional separation techniques and time-of-flight mass spectrometry.
300 $a 144 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0688.
500 $a Chair: David M. Lubman.
502 $a Thesis (Ph.D.)--University of Michigan, 2003.
520 $a In this work, a two-dimensional liquid-phase separation technique coupled with time-of-flight mass spectrometry (TOF-MS) is presented for proteomic studies of human breast cancer. Preparative liquid isoelectric focusing was performed as the first dimension, and nonporous silica reverse-phase high-performance liquid chromatography (NPS RP-HPLC) as the second dimension. NPS RP-HPLC was directly coupled with electrospray ionization (ESI) TOF-MS to obtain accurate intact protein molecular weights. Furthermore, mass fingerprinting and tandem mass spectrometry were performed on tryptic digests of proteins using matrix-assisted laser desorption ionization (MALDI) TOF-MS.
520 $a Human breast epithelial cell lines were studied from a xenograft model of progressive proliferative breast disease. This model consists of the normal MCF10A breast epithelial cells and includes both premalignant and fully malignant variants derived from MCF10A. Proteomic analysis was performed for contribution to breast epithelial protein databases, identification of breast cancer biomarkers, and structural characterization of oncoproteins. This research has resulted in positive identification of over fifty proteins in normal and fully malignant cells. Some of these proteins were found to be differentially expressed between the two cell lines, and represent potential breast cancer biomarkers. Furthermore, studies were conducted on the effect of estradiol on protein expression in premalignant cells. Proteins were identified, including some known oncoproteins, that were differentially expressed in the premalignant cells with estradiol (MCF10AT1E), compared to the MCF10AT and the fully malignant CA1d.cl1 cells. Structural analysis was performed on the oncoproteins p60 c-src and posttranslational modification differences were found between MCF10AT1E and MCF10AT1.
590 $a School code: 0127.
650 4 $a Chemistry, Analytical. $3 586156
650 4 $a Health Sciences, Oncology. $3 1018566
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0486
690 $a 0992
690 $a 0487
710 2 0 $a University of Michigan. $3 777416
773 0 $t Dissertation Abstracts International $g 64-02B.
790 1 0 $a Lubman, David M., $e advisor
790 $a 0127
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3079455