Abstract
Abstract A temperature sensitive protein (one of several) that was soluble at 2°C but reversibly precipitated upon warming to room temperature was isolated from dog milk by precipitation with 50% saturated ammonium sulfate, ion exchange chromatography, centrifugation at 30°C and preparative isoelectric focusing in polyacrylamide gel. The molecular weight by sedimentation equilibrium was 13, 400; however, by thin layer gel filtration it appeared to be much larger. Ultracentrifu-gation studies at conditions near those at which the protein precipitated revealed no evidence of aggregation. The protein had a fairly high content of nonpolar amino acids with proline being in the highest amount. The effects of pH, ionic strength, heat and ethanol on the solubility of the protein were studied. A circular dichroism spectrum of the temperature sensitive protein indicated that the protein is quite unordered. An antiserum against the temperature sensitive protein reacted with each of the other temperature sensitive pr...
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