Improved recovery of methionine after acid hydrolysis using mercaptoethanol

Keutmann, Henry T.; Potts, JT

doi:10.1016/0003-2697(69)90300-5

Cited by 121 publications

(29 citation statements)

References 13 publications

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“…7 N hydrochloric acid containing 0.05% 2-mercaptoethanol in a evacuated sealed tube at 105°C for 24 hr. 3 l Automated amino acid analyses were performed with a JEOL JLC-6AH amino acid analyzer according to the method of Spackman et af. 4 l Other methods.…”

Section: Amino Acid Analysesmentioning

confidence: 99%

Amino Acid Sequence Determination of Nine Tryptic Peptides from Ile Chain of Ricin D

Yoshitake

Funatsu

1978

Agricultural and Biological Chemistry

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Section: Amino Acid Analysesmentioning

confidence: 99%

Amino Acid Sequence Determination of Nine Tryptic Peptides from Ile Chain of Ricin D

Yoshitake

Funatsu

1978

Agricultural and Biological Chemistry

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“…The latter were performed on a Beckman-Spinco automatic amino-acid analyzer, model 120B or 121, adapted for high sensitivity (32) and a rapid elution schedule (33). Hydrolyses were performed at 1100 for 24 hr in constant-boiling HCl (5.7 N) containing 2-mercaptoethanol (1/2000, v/v) (34). ApoA-II was reduced with 2-mercaptoethanol and alkylated with iodoacetic acid (29).…”

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confidence: 99%

Lipid-Protein Interactions in High Density Lipoproteins

Assmann

Brewer

1974

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

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Delipidated high density lipoprotein (apo-HDL), isolated apolipoproteins apoA-I and apoA-II, Scarboxymethylated apoA-II, apoC-I1, the NH2-and CO-OH-terminal CNBr peptides of apoA-II, and the COOH_ terminal CNBr peptide of apoA-I were recombined in vitro with [N-C3H3-cholinelphosphatidylcholine (PC) and (SPM). The It has been shown (1-4) that the protein moiety of human serum high density lipoprotein (HDL), prepared in its lipidfree form (apoHDL) by treatment with organic solvents (5, 6) retains its capacity to bind lipids, both in vivo (7) and in vitro (3,8). About 90% of the protein moiety of apoHDL is composed of two major apoproteins, designated as apoA-I and apoA-II, or, by their COOH-terminal amino acids, as apoGln-I and apoGln-JI (9-16); the remaining 10% is mainly composed of three minor apoproteins (apoC-I, apoC-II, and apoC-III), also associated with the very low density lipolprotein family (9). The complete amino-acid sequences of apoA-II, apoC-I, and apoC-III have been reported (17)(18)(19) 1.063 and 1.210 g/ml, and delipidated with chloroformmethanol, 2:1 (6). The procedures used in the isolation and characterization of the individual proteins of apoHDL are described elsewhere (6). ApoA-I was isolated by chromatography of apoHDL in 6 M urea on Sephadex G-200 (Pharmacia, superfine) (13). ApoA-II was isolated by chromatography of apoHDL in 6 M'\ urea on DEAE-cellulose (Whatman, DE-52) (6, 12). ApoC-III was isolated as described (27,28). Cleavage with CNBr (Eastman, ratio of reagent to peptide, 500: 1) was performed in 70% formic acid at 250 for 48 hr (29). The resulting peptide fragments of apoA-II were purified to homogeneity by chromatography on Sephadex G-75 (0.2 M Tris*HCI, pH 8.6, 6 M urea); peptides of apoA-I, by chromatography on Biogel P-10 (25% acetic acid). ApoA-I, apoA-IJ, COOH-and

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“…Proteins were hydrolyzed for 24 h at 110°C in 0.5 ml of constant boiling 6 N HCI containing 2-mercaptoethanol (1:2,000, vol/vol) (38).…”

Section: Methodsmentioning

confidence: 99%

Properties of the Plasma Very Low and Low Density Lipoproteins in Tangier Disease

Heinen¹,

Herbert²,

Fredrickson³

et al. 1978

J. Clin. Invest.

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Improved recovery of methionine after acid hydrolysis using mercaptoethanol

Cited by 121 publications

References 13 publications

Amino Acid Sequence Determination of Nine Tryptic Peptides from Ile Chain of Ricin D

Amino Acid Sequence Determination of Nine Tryptic Peptides from Ile Chain of Ricin D

Lipid-Protein Interactions in High Density Lipoproteins

Properties of the Plasma Very Low and Low Density Lipoproteins in Tangier Disease

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