Abstract
1. 1. Butyryl-CoA synthetase extracted from untreated or freeze-dried liver mitochondria consisted of two fractions of M, 40,000 and 46,000 as determined by gel permeation chromatography, the higher value Being connrmed Dy sedimentation equilibrium. 2. 2. A red pigment having the characteristics of haem was associated with the enzyme. This appeared to be an artifact of isolation. 3. 3. A number of active bands were obtained on polyacrylamide gel electrophoresis and isoelectric focusing, and on treatment with sodium dodecylsulphate or 6 M guanidine hydrochloride both dissociation and aggregation of the enzyme fractions occurred. 4. 4. As no evidence of protease contamination or proteolytic action could be detected, it is suggested that the active enzymes contain more than one polypeptide chain. © 1984.
| Original language | English |
|---|---|
| Pages (from-to) | 305-314 |
| Number of pages | 10 |
| Journal | International Journal of Biochemistry |
| Volume | 16 |
| Issue number | 3 |
| Publication status | Published - 1984 |
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Ox liver butyryl-coenzyme a synthetase-a subunit enzyme? / Campbell, Callum J.; Park, Milton V.
In: International Journal of Biochemistry, Vol. 16, No. 3, 1984, p. 305-314.Research output: Contribution to journal › Article
TY - JOUR
T1 - Ox liver butyryl-coenzyme a synthetase-a subunit enzyme?
AU - Campbell, Callum J.
AU - Park, Milton V.
PY - 1984
Y1 - 1984
N2 - 1. 1. Butyryl-CoA synthetase extracted from untreated or freeze-dried liver mitochondria consisted of two fractions of M, 40,000 and 46,000 as determined by gel permeation chromatography, the higher value Being connrmed Dy sedimentation equilibrium. 2. 2. A red pigment having the characteristics of haem was associated with the enzyme. This appeared to be an artifact of isolation. 3. 3. A number of active bands were obtained on polyacrylamide gel electrophoresis and isoelectric focusing, and on treatment with sodium dodecylsulphate or 6 M guanidine hydrochloride both dissociation and aggregation of the enzyme fractions occurred. 4. 4. As no evidence of protease contamination or proteolytic action could be detected, it is suggested that the active enzymes contain more than one polypeptide chain. © 1984.
AB - 1. 1. Butyryl-CoA synthetase extracted from untreated or freeze-dried liver mitochondria consisted of two fractions of M, 40,000 and 46,000 as determined by gel permeation chromatography, the higher value Being connrmed Dy sedimentation equilibrium. 2. 2. A red pigment having the characteristics of haem was associated with the enzyme. This appeared to be an artifact of isolation. 3. 3. A number of active bands were obtained on polyacrylamide gel electrophoresis and isoelectric focusing, and on treatment with sodium dodecylsulphate or 6 M guanidine hydrochloride both dissociation and aggregation of the enzyme fractions occurred. 4. 4. As no evidence of protease contamination or proteolytic action could be detected, it is suggested that the active enzymes contain more than one polypeptide chain. © 1984.
UR - http://www.scopus.com/inward/record.url?scp=0021297545&partnerID=8YFLogxK
M3 - Article
VL - 16
SP - 305
EP - 314
JO - International Journal of Biochemistry
JF - International Journal of Biochemistry
SN - 0020-711X
IS - 3
ER -