Purification and characterization of variants of acyl-CoA-binding protein in the bovine liver

M. S. Jensen, P. Hojrup, J. T. Rasmussen, J. Knudsen*

*Kontaktforfatter for dette arbejde

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Four differently modified forms of acyl-CoA-binding protein (ACBP) were identified in ACBP purified from bovine liver. The majority of the purified ACBP was focused at pH 5.9 in isoelectric focusing and could be shown to be N-acetylated AC 13P without any further modifications. Two minor peaks were focused at pH 5.25 and 4.85 respectively. Mass spectrometry and sequence determination showed that the pI 5.25 form was acetylated at Lys 18 and that the pI 4.85 form was malonylated in the same position. Furthermore, it could be shown that non-enzymic glycosylation occurred during purification. The acetylated and malonylated variants of ACBP were only found in adult cattle.

OriginalsprogEngelsk
TidsskriftBiochemical Journal
Vol/bind284
Udgave nummer3
Sider (fra-til)809-812
Antal sider4
ISSN0264-6021
DOI
StatusUdgivet - 1. jan. 1992

Fingeraftryk

Diazepam Binding Inhibitor
Liver
Purification
Glycosylation
Mass spectrometry
Sequence Analysis

Citer dette

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title = "Purification and characterization of variants of acyl-CoA-binding protein in the bovine liver",
abstract = "Four differently modified forms of acyl-CoA-binding protein (ACBP) were identified in ACBP purified from bovine liver. The majority of the purified ACBP was focused at pH 5.9 in isoelectric focusing and could be shown to be N-acetylated AC 13P without any further modifications. Two minor peaks were focused at pH 5.25 and 4.85 respectively. Mass spectrometry and sequence determination showed that the pI 5.25 form was acetylated at Lys 18 and that the pI 4.85 form was malonylated in the same position. Furthermore, it could be shown that non-enzymic glycosylation occurred during purification. The acetylated and malonylated variants of ACBP were only found in adult cattle.",
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Purification and characterization of variants of acyl-CoA-binding protein in the bovine liver. / Jensen, M. S.; Hojrup, P.; Rasmussen, J. T.; Knudsen, J.

I: Biochemical Journal, Bind 284, Nr. 3, 01.01.1992, s. 809-812.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Purification and characterization of variants of acyl-CoA-binding protein in the bovine liver

AU - Jensen, M. S.

AU - Hojrup, P.

AU - Rasmussen, J. T.

AU - Knudsen, J.

PY - 1992/1/1

Y1 - 1992/1/1

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AB - Four differently modified forms of acyl-CoA-binding protein (ACBP) were identified in ACBP purified from bovine liver. The majority of the purified ACBP was focused at pH 5.9 in isoelectric focusing and could be shown to be N-acetylated AC 13P without any further modifications. Two minor peaks were focused at pH 5.25 and 4.85 respectively. Mass spectrometry and sequence determination showed that the pI 5.25 form was acetylated at Lys 18 and that the pI 4.85 form was malonylated in the same position. Furthermore, it could be shown that non-enzymic glycosylation occurred during purification. The acetylated and malonylated variants of ACBP were only found in adult cattle.

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JO - Biochemical Journal

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