scholarly journals Rat heart fatty acid-binding protein. Evidence that supports the amino acid sequence predicted from the cDNA

1989 ◽  
Vol 260 (1) ◽  
pp. 303-306 ◽  
Author(s):  
H Kimura ◽  
M Hitomi ◽  
S Odani ◽  
T Koide ◽  
M Arakawa ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Species ◽  
Rat Heart ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Actual Existence

The amino acid sequence of rat heart fatty acid-binding protein was re-examined by analysing the tryptic and the chymotryptic peptides, since some discrepancies have been reported between the sequences determined by protein analyses and that deduced from the cDNA analyses. Our result completely agreed with the amino acid sequence predicted from the cDNA analyses, providing evidence for the actual existence of the molecular species predicted from the cDNA.

Revision of the amino acid sequence of human heart fatty acid-binding protein

1990 ◽  
pp. 127-133
Author(s):  
Torsten Börchers ◽  
Peter Højrup ◽  
Søren U. Nielsen ◽  
Peter Roepstorff ◽  
Friedrich Spener ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Heart ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Isolation and characterization of fatty acid binding proteins from mammary tissue of lactating rats

1988 ◽  
Vol 251 (3) ◽  
pp. 919-925 ◽  
Author(s):  
P D Jones ◽  
A Carne ◽  
N M Bass ◽  
M R Grigor
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Rat Heart ◽  
Binding Proteins ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding Proteins ◽  
Mammary Tissue ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

A protein fraction with fatty acid binding activity has been isolated from mammary tissue from lactating rats by a process involving DEAE-cellulose ion-exchange chromatography, heat treatment, CM-cellulose ion-exchange chromatography and finally ammonium sulphate precipitation. The purified fraction migrated as a single band on SDS/polyacrylamide-gel electrophoresis with an apparent molecular mass of 14400. However, when this protein fraction was electrophoresed under non-dissociating conditions, two species were observed in a 4:1 ratio. The two components were separated using h.p.l.c. Both bind fatty acids and appear to have similar amino acid compositions although exhibiting different pI values of 4.8 and 4.9. The mammary fatty acid binding proteins appear to be very similar to the fatty acid binding protein isolated from rat heart based on the electrophoretic mobilities and amino acid composition. The major mammary form (pI 4.9) has been partially sequenced and the amino acid sequences obtained can be aligned with 67 residues of the revised rat heart amino acid sequence [Heuckeroth, Birkenmeier, Levin & Gordon (1987) J. Biol. Chem. 262, 9709-9717]. Both mammary species also showed immunochemical identity to rat heart fatty acid binding protein when tested with an anti-serum raised against the heart protein. Anti-sera raised against the minor mammary form (pI 4.8) specifically precipitated this form under non-denaturing conditions but both forms after they had been denatured. Quantitative immunoassays using the anti-(heart fatty acid binding protein) serum showed that concentrations of the fatty acid binding proteins present in mammary cytosols increase during lactation and increase further after feeding a high-fat diet.

Revision of the amino acid sequence of human heart fatty acid-binding protein

1990 ◽  
Vol 98 (1-2) ◽  
Author(s):  
Torsten B�rchers ◽  
Peter H�jrup ◽  
S�renU. Nielsen ◽  
Peter Roepstorff ◽  
Friedrich Spener ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Heart ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Characterization and amino acid sequence of a fatty acid-binding protein from human heart

1988 ◽  
Vol 252 (1) ◽  
pp. 191-198 ◽  
Author(s):  
G D Offner ◽  
P Brecher ◽  
W B Sawlivich ◽  
C E Costello ◽  
R F Troxler
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Heart ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Amino Acid Sequences ◽  
British Library ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

The complete amino acid sequence of a fatty acid-binding protein from human heart was determined by automated Edman degradation of CNBr, BNPS-skatole [3′-bromo-3-methyl-2-(2-nitrobenzenesulphenyl)indolenine], hydroxylamine, Staphylococcus aureus V8 proteinase, tryptic and chymotryptic peptides, and by digestion of the protein with carboxypeptidase A. The sequence of the blocked N-terminal tryptic peptide from citraconylated protein was determined by collisionally induced decomposition mass spectrometry. The protein contains 132 amino acid residues, is enriched with respect to threonine and lysine, lacks cysteine, has an acetylated valine residue at the N-terminus, and has an Mr of 14768 and an isoelectric point of 5.25. This protein contains two short internal repeated sequences from residues 48-54 and from residues 114-119 located within regions of predicted beta-structure and decreasing hydrophobicity. These short repeats are contained within two longer repeated regions from residues 48-60 and residues 114-125, which display 62% sequence similarity. These regions could accommodate the charged and uncharged moieties of long-chain fatty acids and may represent fatty acid-binding domains consistent with the finding that human heart fatty acid-binding protein binds 2 mol of oleate or palmitate/mol of protein. Detailed evidence for the amino acid sequences of the peptides has been deposited as Supplementary Publication SUP 50143 (23 pages) at the British Library Lending Division, Boston Spa, Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1988) 249, 5.

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