NDLI: Escherichia coli ß-galactosidase is heterogeneous with respect to a requirement for magnesium

Content Provider	Springer Nature Link
Author	Craig, Douglas B. Hall, Tara Goltz, Douglas M.
Copyright Year	2000
Abstract	Commercially obtained E. coli ß-galactosidase was stored at 25 °C in buffer containing 1 mM MgCl2 and in buffer containing no added MgCl2. Samples were removed at set times and the activity of individual enzyme molecules assayed. When stored in the presence of 1 mM magnesium, the number of active molecules did not change over a 2.5-h period. When stored in the absence of added MgCl2, over half the enzyme molecules became inactive within the first hour. However, those molecules which retained activity remained active for the duration of the experiment. This indicates that there may exist two populations of E. coli ß-galactosidase, one which requires storage in the presence of the higher concentration of Mg2+ in order to remain active. There was no observed correlation between this requirement for magnesium and reaction rate. Additionally, the presence of the 1 mM MgCl2 was found to decrease the average activity of the ß-galactosidase molecules under the conditions employed.
Starting Page	223
Ending Page	229
Page Count	7
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	13
Issue Number	3
e-ISSN	15728773
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2000-01-01
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Physical Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Selenium metabolism in Escherichia coli

Magnesium chemistry and biochemistry

Intracellular magnesium and magnesium buffering

Genetic disorders of magnesium homeostasis

Escherichia coli topoisomerase I is an iron and zinc binding protein

Structural and catalytic chemistry of magnesium-dependent enzymes

Preface – Introduction – Magnesium in the New Millenium

Structure, properties and regulation of magnesium transport proteins

Quantitative proteomic profiling of the Escherichia coli response to metallic copper surfaces

Escherichia coli ß-galactosidase is heterogeneous with respect to a requirement for magnesium

Similar Documents

Selenium metabolism in Escherichia coli

Magnesium chemistry and biochemistry

Intracellular magnesium and magnesium buffering

Genetic disorders of magnesium homeostasis

Escherichia coli topoisomerase I is an iron and zinc binding protein

Structural and catalytic chemistry of magnesium-dependent enzymes

Preface – Introduction – Magnesium in the New Millenium

Structure, properties and regulation of magnesium transport proteins

Quantitative proteomic profiling of the Escherichia coli response to metallic copper surfaces

Escherichia coli ß-galactosidase is heterogeneous with respect to a requirement for magnesium