Determination of the amino acid sequence of the C-terminal cyanogen bromide fragment of myoglobin from bottle nosed dolphin by mass spectrometric peptide mixture analysis

Roepstorff, Peter

doi:10.1002/bms.1200050508

Cited by 9 publications

(5 citation statements)

References 23 publications

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“…Peptides (about 60 nmol) were acetylated with acetic anhydride/methanol, 1:3 (vol/vol) for 30 min. Permethylation and pertrideuteriomethylation were performed as described (20) but with reaction times decreased to 1 min to avoid sulfonium salt formation at CMCys (21). The electron-impact mass spectra were obtained by direct introduction (probe temp, 230-2700C) on a Finnigan MAT 311A mass spectrometer interfaced to a Finnigan MAT SS200 data system.…”

Section: Methodsmentioning

confidence: 99%

beta-Hydroxyaspartic acid in vitamin K-dependent protein C.

Drakenberg¹,

Fernlund²,

Roepstorff³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

137

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Previous work has shown that the light chain of protein C, an anticoagulant plasma protein, contains an unusual amino acid [Fernlund, P. & Stenflo, J. (1982) J. Biol. Chem. 257, 12170-12179]. To determine the structure of this amino acid a heptapeptide, CMCys-Ile-X-Gly-Leu-Gly-Gly (residues 69-75 in the light chain), was isolated from enzymatic digests of the light chain. According to automatic Edman sequence analysis, 1H NMR spectroscopy, and mass spectrometry the heptapeptide had beta-hydroxyaspartic acid in its third position, which corresponds to position 71 in the light chain of protein C. Analysis of acid and aminopeptidase M hydrolysates of the heptapeptide showed the beta-hydroxyaspartic acid to be the erythro form. Acid hydrolysis of protein C released approximately equal to 1 mol of beta-hydroxyaspartic acid per mol of protein. The function of this amino acid, which, to the best of our knowledge, has not been found previously in proteins, is unknown.

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Section: Methodsmentioning

confidence: 99%

beta-Hydroxyaspartic acid in vitamin K-dependent protein C.

Drakenberg¹,

Fernlund²,

Roepstorff³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

137

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“…The sample (approx. 10-20 nmol) was N-acetylated and NO-permethylated by the procedure previously described (Roepstorff, 1978).…”

Section: Amino Acid Analysismentioning

confidence: 99%

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

Knudsen¹,

Højrup²,

Hansen³

et al. 1989

Biochemical Journal

147

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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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“…The sample (approx. 10-15 nmol) was N-[2H3]acetylated and NO-permethylated by using the procedure previously described (Roepstorff, 1978).…”

Section: Mass Spectrometrymentioning

confidence: 99%