| Original language | English (US) |
|---|---|
| Pages (from-to) | 186-189 |
| Number of pages | 4 |
| Journal | BBA - Enzymology |
| Volume | 167 |
| Issue number | 1 |
| DOIs | |
| State | Published - Aug 27 1968 |
| Externally published | Yes |
ASJC Scopus subject areas
- General Medicine
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In: BBA - Enzymology, Vol. 167, No. 1, 27.08.1968, p. 186-189.
Research output: Contribution to journal › Article › peer-review
}
TY - JOUR
T1 - Betainealdehyde dehydrogenase
T2 - assay and partial purification
AU - Goldberg, A. M.
AU - McCaman, R. E.
N1 - Funding Information: This work was supported by a grant from the Japanese Ministry of Education for scientific research. Funding Information: buffer at pH 8.1 about 90% of optimum activity is obtained. Phosphate buffers at this same pH are inhibitory. Betaine aldehyde in a concentration of I mM gave maximum activity. Increasing the concentration to IO mM caused a slight decrease in the activity of the enzyme (Fig, I). The apparent Kin, obtained by a Lineweaver-Burk plot, is 2.6" lO -4 M, (Fig. I) which is in excellent agreement with that obtained by ROTHSCHILD AND GUZMAN-BARRON 3. The preparation described was tested as to the "specificity" of the aldehyde dehydrogenase. All conditions were as described above, except that different aldehydes were substituted for the betaine aldehyde in the same final concentration. The rate of oxidation of acetylaldehyde and propionaldehyde was less than lO% of that for betaine aldehyde. The low activity toward acetaldehyde suggests that non-specific aldehyde dehydrogenases have been removed to a considerable extent. The primary purpose of this study was to isolate a partially purified dehydrogenase that could be used in the development of an assay system for choline dehydrogenase. The partial purification of choline dehydrogenase is now in progress and it is expected that these two enzymes may be of considerable use in developing a sensitive fluorometric method for endogenous choline and acetylcholine in tissue extracts. This investigation was supported in part by Public Health Service Grant MH 10695 and a grant from the National Multiple Sclerosis Society (347)-
PY - 1968/8/27
Y1 - 1968/8/27
UR - http://www.scopus.com/inward/record.url?scp=0014432258&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0014432258&partnerID=8YFLogxK
U2 - 10.1016/0005-2744(68)90290-8
DO - 10.1016/0005-2744(68)90290-8
M3 - Article
C2 - 5686290
AN - SCOPUS:0014432258
SN - 0005-2744
VL - 167
SP - 186
EP - 189
JO - BBA - Enzymology
JF - BBA - Enzymology
IS - 1
ER -