Fatty acid-binding protein in bovine longissimus dorsi muscle. Academic Article

abstract

• Experiments were conducted to purify and obtain amino acid sequence data for fatty acid-binding protein from bovine longissimus dorsi muscle. 1. Separation of sarcoplasmic proteins by fractionation on Sephadex and DEAE cellulose columns indicated that a low abundance fatty acid-binding protein exists in bovine l. dorsi muscle. 2. Fatty acid-binding protein in bovine l. dorsi muscle cannot be separated from myoglobin by standard protein purification procedures. However, partial sequencing of a partially purified protein fraction indicated the presence of an NH2-terminally blocked protein. 3. Myoglobin bound palmitate under the in vitro conditions of these experiments.

authors

• Smith, Stephen

published proceedings

• Comp Biochem Physiol B

author list (cited authors)

• Moore, K. K., Cameron, P. J., Ekeren, P. A., & Smith, S. B.

citation count

• 10

complete list of authors

• Moore, KK||Cameron, PJ||Ekeren, PA||Smith, SB

publication date

• January 1993

publisher

• Elsevier  Publisher

published in

• Comparative Biochemistry and Physiology - B: Comparative Biochemistry  Journal

keywords

• Amino Acid Sequence
• Amino Acids
• Animals
• Carrier Proteins
• Cattle
• Chromatography, Gel
• Chromatography, Ion Exchange
• Electrophoresis, Polyacrylamide Gel
• Fatty Acid-binding Proteins
• Fatty Acids
• Female
• Male
• Molecular Sequence Data
• Muscles
• Neoplasm Proteins
• Sequence Homology, Amino Acid

Digital Object Identifier (DOI)

• 10.1016/0305-0491(93)90366-d

start page

• 259

end page

• 266

volume

• 104

issue

• 2

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2F0305-0491%2893%2990366-d