Tools

LEADER 03586ctm a2200541 i 4500

001 ocm48651172;

003 OCoLC;

005 20250120152107.0;

008 011220s2001 xx a bm 000 0 eng d;

035 a| (Sirsi) o48651172;

035 a| (OCoLC)48651172;

049 a| EREE;

050 4 a| QP752.B54b| J67 2001;

100 1 a| Jordan, Rick Matthew,e| author.?| UNAUTHORIZED;

245 10 a| Cloning and characterization of a conjugated bile acid hydrolase gene from enterococcus faecalis /c| by Rick Matthew Jordan.;

264 0 c| 2001.;

300 a| x, 64 leaves :b| illustrations (some color) ;c| 28 cm;

336 a| textb| txt2| rdacontent;

337 a| unmediatedb| n2| rdamedia;

338 a| volumeb| nc2| rdacarrier;

502 b| M.S.c| East Carolina Universityd| 2001;

500 a| Presented to the faculty of the Department of Biology.;

500 a| Advisor: James P. Coleman;

520 3 a| Sequence analysis of a partial genome sequence of Enterococcus faecalis indicated the presence of an open reading frame (ORE) with homology to members of the conjugated bile acid hydrolase/ penicillin V amidase family. In order to define the function of this ORE, a genomic DNA fragment was cloned containing this sequence from Enterococcus faecalis, and its nucleotide sequence was confirmed. The DNA fragment was amplified using primers based on the flanking sequence, ligated into pUC19, and transformed into E. coli. Colonies containing inserts were streaked to purity and assayed for conjugated bile acid hydrolase activity. Plasmid DNA was subjected to automated DNA sequencing to confirm the genomic sequencing data. Following purification of the enzyme expressed in E. coli, substrate specificity assays demonstrated that the enzyme is a conjugated bile acid hydrolase. Activity was higher on glycine conjugates than on taurine conjugates. No hydrolytic activity toward penicillin V was observed. The enzyme displayed optimal bile acid hydrolysis at a pH of 5.0. Therefore, results confirm that this gene encodes a conjugated bile acid hydrolase, rather than a penicillin V amidase.;

504 a| Includes bibliographical references (leaves 61-64).;

650 0 a| Bile acidsx| Physiology.=| ^A32181;

650 0 a| Gene expression.=| ^A6250;

650 0 a| DNA.=| ^A8939;

650 0 a| Enterococcus faecalis.=| ^A503836;

650 7 a| DNA.2| fast0| (OCoLC)fst00886555;

650 7 a| Enterococcus faecalis.2| fast0| (OCoLC)fst00912613;

650 7 a| Gene expression.2| fast0| (OCoLC)fst00939613;

655 7 a| dissertations.2| aat0| (CStmoGRI)aatgf300028029;

655 7 a| Academic theses.2| fast0| (OCoLC)fst01726453;

655 7 a| Academic theses.2| lcgft;

655 7 a| Thèses et écrits académiques.2| rvmgf0| (CaQQLa)RVMGF-000001173;

700 1 a| Coleman, James P.,e| degree supervisor.=| ^A1461136;

710 2 a| East Carolina University.b| Department of Biology.=| ^A637467;

856 41 z| Access via ScholarShipu| http://hdl.handle.net/10342/12534;

949 a| Click on web addressw| asish| joyner101;

949 a| Click on web addressw| asish| hsl111;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 863591;

999 a| ASK AT SPECIAL COLLECTIONS DESKw| ASISc| 1i| 1422883d| 3/12/2003l| JSCJTHDm| JOYNERr| Ys| Yt| JSCJTHDu| 1/8/2002x| ETDz| JSPECCOLLo| .STAFF. 0;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 863591-3001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 12/13/2024x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 863591-4001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 12/13/2024x| ETDz| HERESOURCE;

Cloning and characterization of a conjugated bile acid hydrolase gene from enterococcus faecalis / by Rick Matthew Jordan.

Author/creator	Jordan, Rick Matthew author.
Other author	Coleman, James P., degree supervisor.
Other author	East Carolina University. Department of Biology.
Format	Theses and dissertations
Production	2001.
Description	x, 64 leaves : illustrations (some color) ; 28 cm
Supplemental Content	Access via ScholarShip
Subjects	Bile acids--Physiology. Gene expression. DNA. Enterococcus faecalis.

Summary	Sequence analysis of a partial genome sequence of Enterococcus faecalis indicated the presence of an open reading frame (ORE) with homology to members of the conjugated bile acid hydrolase/ penicillin V amidase family. In order to define the function of this ORE, a genomic DNA fragment was cloned containing this sequence from Enterococcus faecalis, and its nucleotide sequence was confirmed. The DNA fragment was amplified using primers based on the flanking sequence, ligated into pUC19, and transformed into E. coli. Colonies containing inserts were streaked to purity and assayed for conjugated bile acid hydrolase activity. Plasmid DNA was subjected to automated DNA sequencing to confirm the genomic sequencing data. Following purification of the enzyme expressed in E. coli, substrate specificity assays demonstrated that the enzyme is a conjugated bile acid hydrolase. Activity was higher on glycine conjugates than on taurine conjugates. No hydrolytic activity toward penicillin V was observed. The enzyme displayed optimal bile acid hydrolysis at a pH of 5.0. Therefore, results confirm that this gene encodes a conjugated bile acid hydrolase, rather than a penicillin V amidase.
General note	Presented to the faculty of the Department of Biology.
General note	Advisor: James P. Coleman
Dissertation note	M.S. East Carolina University 2001
Bibliography note	Includes bibliographical references (leaves 61-64).
Genre/form	dissertations.
Genre/form	Academic theses.
Genre/form	Academic theses.
Genre/form	Thèses et écrits académiques.

Availability

Library	Location	Call Number	Status	Item Actions
Joyner	University Archives	ASK AT SPECIAL COLLECTIONS DESK	✔ Available	Request Material
	Electronic Resources	Access Content Online	✔ Available

Cloning and characterization of a conjugated bile acid hydrolase gene from enterococcus faecalis / by Rick Matthew Jordan.

Click here for more information about this title

Availability