The Japanese Journal of Pediatric Dentistry
Online ISSN : 2186-5078
Print ISSN : 0583-1199
ISSN-L : 0583-1199
Purification of LDH Isozyme from Pig Dental Pulp
Naoyoshi SatoYuzuru YoshimuraKenichi SuseAkira SuzukiMikako YoshidaEtsuko ChibaHideo Goto
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Keywords: LDH isozyme
JOURNAL FREE ACCESS

1994 Volume 32 Issue 5 Pages 1137-1144

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Abstract
Lactate dehydrogenase (EC.1.1.1.27; LDH) catalyzes the conversion between pyruvate and L-lactate as the last step of the glycoytic pathway. We devised methods for the separation and purification of dental pulp LDH isozyme from the first molar (M1) of pigs.
LDH-1 isozyme was purified to a specific activity of 442.2 units/mg of protein, representing an approximately 1580-fold purification from the crude extract, using DEAE Sephadex A-50 column chromatography and Blue dextran affinity chromatography. LDH-2 and 3 isozyme were also highly purified and high recovery.
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© The Japanese Society of Pediatric Dentistry
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