scholarly journals Amino acid sequence of acyl-CoA-binding protein from cow liver

1987 ◽  
Vol 245 (3) ◽  
pp. 857-861 ◽  
Author(s):  
J Mikkelsen ◽  
P Højrup ◽  
P F Nielsen ◽  
P Roepstorff ◽  
J Knudsen
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gas Phase ◽  
Fast Atom Bombardment ◽  
Binding Protein ◽  
Bovine Liver ◽  
Plasma Desorption ◽  
Flight Mass Spectrometry

Acyl-CoA-binding protein from bovine liver was purified with the use of reverse-phase h.p.l.c. in the final step. The complete amino acid sequence was determined by using a combination of gas-phase Edman degradation and electron-impact and fast-atom-bombardment mass spectrometry. The sequence was confirmed by determination of the Mr by plasma-desorption time-of-flight mass spectrometry.

scholarly journals Determination of the Complete Amino Acid Sequence for the Coat Protein of Brome Mosaic Virus by Time-of-Flight Mass Spectrometry

2001 ◽  
Vol 276 (23) ◽  
pp. 20039-20047 ◽  
Author(s):  
Yi-Min She ◽  
Steve Haber ◽  
Dallas L. Seifers ◽  
Alexander Loboda ◽  
Igor Chernushevich ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Mosaic Virus ◽  
Time Of Flight ◽  
Brome Mosaic Virus ◽  
Complete Amino Acid Sequence ◽  
Flight Mass Spectrometry

The amino acid sequence of porcine intestinal calcium-binding protein

1979 ◽  
Vol 57 (6) ◽  
pp. 737-748 ◽  
Author(s):  
Theo Hofmann ◽  
Michiko Kawakami ◽  
Anthony J. W. Hitchman ◽  
Joan E. Harrison ◽  
Keith J. Dorrington
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intestinal Mucosa ◽  
Calcium Binding ◽  
Binding Protein ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

The complete amino acid sequence of the calcium-binding protein (CaBP) from pig intestinal mucosa has been determined: Ac-Ser-Ala-Gln-Lys-Ser-Pro-Ala-Glu-Leu-Lys-Ser-Ile-Phe-Glu-Lys-Tyr-Ala-Ala-Lys-Glu-Gly-Asp-Pro-Asn-Gln-Leu-Ser-Lys-Glu-Glu-Leu-Lys-Gln-Leu-Ile-Gln-Ala-Glu-Phe-Pro-Ser-Leu-Leu-Lys-Gly-Pro-Arg-Thr-Leu-Asp-Asp-Leu-Phe-Gln-Glu-Leu-Asp-Lys-Asn-Gly-Asn-Gly-Glu-Val-Ser-Phe-Glu-Glu-Phe-Gln-Val-Leu-Val-Lys-Lys-Ile-Ser-Gln-OH. The N-terminal octapeptide sequence was determined by mass spectrometry analysis by Morris and Dell. The first 45 residues of bovine CaBP differ only in six positions from the corresponding sequence of the porcine protein, except that the sequence starts in position two of the porcine sequence. The mammalian intestinal CaBP's belong to the troponin-C superfamily on the basis of an analysis by Barker and Dayhoff.

scholarly journals Acyl-CoA-binding protein in the rat. Purification, binding characteristics, tissue concentrations and amino acid sequence

1989 ◽  
Vol 262 (2) ◽  
pp. 513-519 ◽  
Author(s):  
J Knudsen ◽  
P Højrup ◽  
H O Hansen ◽  
H F Hansen ◽  
P Roepstorff
Keyword(s):  
Mass Spectrometry ◽  
Gas Phase ◽  
Soluble Fraction ◽  
Binding Protein ◽  
Sequence Similarity ◽  
Tissue Concentrations ◽  
Binding Characteristics ◽  
Plasma Desorption Mass Spectrometry ◽  
Plasma Desorption ◽  
Strong Sequence Similarity

Acyl-CoA-binding protein (ACBP) was purified from rat liver. The Mr was determined as 9932 +/- 10 by mass spectrometry and calculated as 9937.8 from the sequence. The protein binds acyl-CoA esters (C8-C16) with high affinity, but was unable to bind fatty acids. ACBP was found mainly (86%) in the soluble fraction, and the concentration was highest in liver, 5-6 micrograms/mg of soluble protein. The complete primary structure was determined by a combination of gas-phase Edman degradations and mass spectrometry. Extensive use of 252Cf plasma-desorption mass spectrometry facilitated the identification and verification of peptides. Comparison with the previously determined sequence of bovine acyl-CoA-binding protein revealed a very strong sequence similarity (83%), and all of the differences could be accounted for by single base changes.

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