Maintenance of quaternary structure in the frozen state stabilizes lactate dehydrogenase during freeze-drying
Journal Article
Overview
publication date
- June 1, 2001
has subject area
- Animals
- Biochemical Phenomena - Enzyme Activation
- Biomedical and Dental Materials - Polymers
- Carbohydrates
- Diagnostic Techniques and Procedures - Freeze Drying
- Diagnostic Techniques and Procedures - Freeze Drying
- Enzymes - Isoenzymes
- Heart - Myocardium
- In Vitro Techniques
- Investigative Techniques - Enzyme Stability
- Investigative Techniques - Freeze Drying
- Investigative Techniques - Freeze Drying
- Investigative Techniques - Freeze Drying
- Lactate Dehydrogenases - L-Lactate Dehydrogenase
- Macromolecular Substances - Polymers
- Manufactured Materials - Polymers
- Metabolism - Enzyme Activation
- Muscle, Striated - Myocardium
- Musculoskeletal System - Muscles
- Musculoskeletal System - Myocardium
- NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases - L-Lactate Dehydrogenase
- Protein Isoforms - Isoenzymes
- Protein Stability - Enzyme Stability
- Protein Structure, Quaternary
- Protein Subunits
- Rabbits
- Salts
- Surface-Active Agents
- Swine
- Therapeutics - Freeze Drying
- Thermodynamics
- Tissues - Muscles
has restriction
- closed
Date in CU Experts
- September 3, 2013 2:48 AM
Full Author List
- Anchordoquy TJ; Izutsu K; Randolph TW; Carpenter JF
author count
- 4
citation count
- 86
published in
Other Profiles
International Standard Serial Number (ISSN)
- 0003-9861
Electronic International Standard Serial Number (EISSN)
- 1096-0384
Digital Object Identifier (DOI)
Additional Document Info
start page
- 35
end page
- 41
volume
- 390
issue
- 1