Dry Thermal Inactivation of Trypsin and Ribonuclease
نویسندگان
چکیده
منابع مشابه
[A study of the dry thermal denaturation of ribonuclease].
Unsere Befunde widersprechen hinsichtlich der Vorkommen von antezso-Fettsäuren mit gerader Gesamt-C-Zahl und den ungesättigten verzweigten Fettsäuren denen v o n WHITE und FREERMAN2 . O b w o h l es naheliegend wäre, diese Divergenzen auf Unterschiede des Staphylococcen-Stammes zurückzuführen, nehmen wir an, daß die strukturelle Zuordnung v o n W H I T E u n d FREERMAN, d i e n u r au f R e t e...
متن کاملThe Inactivation of Trypsin
1. A study has been made of the equilibrium existing between trypsin and the substances formed in the digestion of proteins which inhibit its action. 2. This substance could not be obtained by the hydrolysis of the proteins by acid or alkali. It is dialyzable. 3. The equilibrium between this substance (inhibitor) and trypsin is found to agree with the equation, trypsin + inhibitor right harpoon...
متن کاملThermal inactivation of eight Salmonella serotypes on dry corn flour.
Dry heat was used to inactivate Salmonella newington, Salmonella typhimurium, Salmonella anatum, Salmonella kentucky, Salmonella cubana, Salmonella seftenberg, Salmonella thompson, and Salmonella tennessee in corn flour at 10 and 15% moisture. The flour was spray inoculated at 10(5) Salmonella cells per g and then stored at 49 degrees C (120 degrees F); viable Salmonella cells were counted on T...
متن کاملInactivation of Crystalline Trypsin
1. The rate of inactivation of crystalline trypsin solutions and the nature of the products formed during the inactivation at various pH at temperatures below 37 degrees C. have been studied. 2. The inactivation may be reversible or irreversible. Reversible inactivation is accompanied by the formation of reversibly denatured protein. This denatured protein exists in equilibrium with the native ...
متن کاملOn the x-ray inactivation at various temperatures of trypsin in dry state and aqueous solution.
für Naturforschung in cooperation with the Max Planck Society for the Advancement of Science under a Creative Commons Attribution 4.0 International License. Dieses Werk wurde im Jahr 2013 vom Verlag Zeitschrift für Naturforschung in Zusammenarbeit mit der Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. digitalisiert und unter folgender Lizenz veröffentlicht: Creative Commons Namen...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nature
سال: 1966
ISSN: 0028-0836,1476-4687
DOI: 10.1038/210953a0