Nε-(dl-2-Amino-2-carboxyethyl)-l-lysine, a New Amino Acid Formed on Alkaline Treatment of Proteins

Bohak, Zvi

doi:10.1016/s0021-9258(18)93828-7

Cited by 267 publications

(39 citation statements)

References 26 publications

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“…The first two have been ascribed to the ionization of tyrosine (Shugar, 1952). The absorption at 241 nm may be due to the formation of sulfide (Donovan and White, 1971) and dehydro amino acids (Bohak, 1964). In the present study it was used as an approximate method to follow the reaction rates.…”

Section: Resultsmentioning

confidence: 99%

“…elimination mechanism in proteins has been presented by Tarbell and Harnish (1951), Swan (1957), Patchornik and Sokolovsky (1964), Sokolovsky et al (1964), Ziegler (1964), Bohak (1964), Corfield et al (1967), Miro and Garcia-Dominguez (1967), and Gawron and Odstrschel (1967), the stoichiometry was never established. We have presented strong evidence by establishing the correct stoichiometry.…”

Section: Discussionmentioning

confidence: 99%

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Effects of alkali on proteins. Disulfides and their products

Nashef¹,

Osuga²,

Lee³

et al. 1977

J. Agric. Food Chem.

158

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Effects of alkali on proteins. Disulfides and their products

Nashef¹,

Osuga²,

Lee³

et al. 1977

J. Agric. Food Chem.

158

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“…Aronson and Fitz-James (3) have considered the possibility of lysinoalanine formation from cysteine and lysine during extraction of coat protein at high pH. Initial studies on this reaction (8) showed that this reaction did not occur at either pH 10.6 during 6 h or pH 7.0 in 0.1 M Tris-hydrochloride (100°C for 30 min). Our extraction procedures (pH 10, 37°C for 20 min, and pH 6.8, 100°C for 3 min) solubilized protein which, upon amino acid analysis, did not reveal the production of lysinoalanine.…”

Section: Discussionmentioning

confidence: 99%

Bacillus subtilis spore coats: complexity and purification of a unique polypeptide component

Goldman¹,

Tipper²

1978

J Bacteriol

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Extensively washed, dormant spores of Bacillus subtilis were disrupted with glass beads in buffer at pH 7 in the presence of protease inhibitors. Approximately 31% of the total spore protein was soluble, and another 14% was removed from the insoluble fraction by hydrolysis with lysozyme and washing with 1 M KCl and 0.1% sodium dodecyl sulfate. The residual spore integuments comprised 55% of the total spore proteins and consisted of coats and residual membrane components. Treatment of integuments with sodium dodecyl sulfate and reducing agents at pH 10 solubilized 40% of the total spore protein. Seven low-molecular-weight polypeptide components of this solubilized fraction comprised 27% of the total spore protein. They are not normal membrane components and reassociated to form fibrillar structures resembling spore coat fragments. The residual insoluble material (15% of the total spore protein) was rich in cysteine and was probably also derived from the spore coats. A solubilized coat polypeptide of molecular weight 12,200 has been purified in good yield (4 to 5% of the total spore protein). Five amino acids account for 92% of its total amino acid residues: glycine, 19%; tyrosine, 31%; proline, 23%; arginine, 13%; and phenylalanine, 6%.

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“…Direct treatment of lysozyme under standard reaction conditions results in the appearance of cysteic acid, although the serine and threonine content remained unchanged. This may be due to elimination-addition prior or subsequent to sulfitolysis of the disulfide bridges (Swan, 1957; Donovan, 1967;Bohak, 1964).…”

Section: Resultsmentioning

confidence: 99%