Isolierung des kristallinen Hauptanteils aus Seidenfibroin. Vorläufige Mitteilung
- 1 January 1954
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 298 (Jahresband) , 239-240
- https://doi.org/10.1515/bchm2.1954.298.1.239
Abstract
Silk is treated with papain, then dissolved in 50% lithium rhodanide and dialyzed. The resulting silk fibroin is treated with crystalline chymotrypsin. This leads to the precipitation of a crystalline peptide containing tyrosine, alanine, serine and glycine in the ratio 1:1:2:3. The amino end group belongs to glycine. The substance is hydrolzed by papain if lithium rhodanide is present. Acid hydrolysis leads to the formation of 3 peptides containing glycine and serine, glycine and tyrosine, and glycine, serine and alanine, respectively.Keywords
This publication has 3 references indexed in Scilit:
- CHROMATOGRAPHY OF AMINO ACIDS ON STARCH COLUMNS. SOLVENT MIXTURES FOR THE FRACTIONATION OF PROTEIN HYDROLYSATESJournal of Biological Chemistry, 1949
- AMINO ACID COMPOSITION OF BETA-LACTOGLOBULIN AND BOVINE SERUM ALBUMIN1949
- CHROMATOGRAPHY OF AMINO ACIDS ON STARCH COLUMNS. SEPARATION OF PHENYLALANINE, LEUCINE, ISOLEUCINE, METHIONINE, TYROSINE, AND VALINEJournal of Biological Chemistry, 1948