ovalbumin and Carcinoma--Krebs-2

Denaturation of hen ovalbumin synthesized in a cell-free system was assayed by examining its sensitivity to trypsin. The native ovalbumin resisted digestion by trypsin, and it remained resistant to digestion when some amino acid analogs, including azetidine-2-carboxylic acid and meta-flourotyrosine, were incorporated into its peptide chain. However, when other amino acid analogs such as beta-hydroxyleucine and 4-thiaisoleucine were incorporated during protein systhesis, ovalbumin became very lablie to trypsin. These experiments demonstrate a sensitive system for detecting protein denaturation and suggest a variable effect of different amino acid analogs on the native conformation of a protein.

Topics: Animals; Carcinoma, Krebs 2; Cell-Free System; Chickens; Female; Mice; Ovalbumin; Protein Denaturation; Ribosomes; RNA, Messenger; Trypsin

Topics: Animals; Carcinoma, Krebs 2; Cell-Free System; Chickens; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Evaluation Studies as Topic; Female; Globins; Leucine; Methods; Ovalbumin; Oviducts; Phenylhydrazines; Polyribosomes; Protein Biosynthesis; Rabbits; Reticulocytes; Ribosomes; RNA, Messenger; Sodium Dodecyl Sulfate; Spectrophotometry, Ultraviolet; Tritium

Topics: Animals; Carcinoma, Krebs 2; Cellulose; Chickens; Chromatography; Electrophoresis, Disc; Globins; Kinetics; Leucine; Macromolecular Substances; Ovalbumin; Oviducts; Peptide Initiation Factors; Precipitin Tests; Protein Biosynthesis; Rabbits; Reticulocytes; Ribosomes; RNA, Messenger; Serine; Sodium Dodecyl Sulfate; Tritium