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Epimerization of trans-4-hydroxy-l-proline to cis-4-hydroxy-d-proline during acid hydrolysis of collagen

1972; Elsevier BV; Volume: 49; Issue: 2 Linguagem: Inglês

10.1016/0003-2697(72)90461-7

1096-0309

Dominic D. Dziewiatkowski, Vincent Hascall, Rick Riolo,

Bone and Dental Protein Studies

1. trans-4-Hydroxy-l-proline is epimerized to cis-4-hydroxy-d-proline under the conditions generally used for the hydrolysis of proteins for analyses of amino acids. 2. The cis epimer elutes from a column of UR-30 resin on a Beckman amino acid analyzer at the same time as threonine and hence would be undetected. 3. About 8% of the trans-4-hydroxy-l-proline in collagen can be epimerized to cis-4-hydroxy-d-proline in the hydrolysis of collagen with 6 N HCl at 110° for 72 hr. 4. A procedure is described whereby the primary amino acids in hydrolyzates are deaminated with nitrous acid and removed so that the amounts of trans-4-hydroxyproline, cis-4-hydroxyproline, and proline can be determined without changing the temperature of the column of UR-30 resin on the Beckman amino acid analyzer.