Purification of Pepsin by Gel Filtration.
نویسندگان
چکیده
منابع مشابه
Purification of an acid alpha-glucosidase by dextran-gel filtration.
1. The behaviour of rat liver alpha-glucosidases on dextran gel (Sephadex G-100) columns was studied. A ;retardation' of an acid alpha-glucosidase activity was observed. This activity was identified as lysosome alpha-(1-->4)-glucosidase. A single gel-filtration step resulted in a 700-fold purification of the enzyme. The same technique was also used to purify the acid alpha-glucosidase of human ...
متن کاملPurification of Pepsin
Since 1836, when Theodor Schwann signalized the presence in gastric juice of the proteolytic ferment which he was the first to designate as pepsin, a large number of attempts have been made to isolate it in a pure form to determine its chemical nature and its ultimate physiological properties. In a large majority of these, and, especially, all those made before 1895, except that of Brticke (I),...
متن کاملPurification of Pepsin
Since 1836, when Theodor Schwann signalized the presence in gastric juice of the proteolytic ferment which he was the first to designate as pepsin, a large number of attempts have been made to isolate it in a pure form to determine its chemical nature and its ultimate physiological properties. In a large majority of these, and, especially, all those made before 1895, except that of Brticke (I),...
متن کاملSeparation of Thyroidal Iodoproteins and Purification of Thyroglobulin by Gel Filtration and Density Gradient Centrifugation.
Thyroglobulin, the major protein component of normal thyroid glands, contains more than 80% of the thyroidal iodine and has been considered the only source of thyroid hormones (1). Aqueous thyroid extracts contain, besides thyroglobulin, other proteins in variable amounts. Essentially, four methods have been used for the characterization of the various components in such extracts and for the pu...
متن کاملPurification of human plasminogen and plasmin by gel filtration on Sephadex and chromatography on diethylaminoethyl-Sephadex.
Highly purified human plasminogen has been prepared from a variety of plasma fractions and by different purification methods. The two major fractions used have been serum or plasma euglobulin and Cohn plasma Fraction III. The purification methods (1-14) have all yielded products of high purity. Plasminogen useful for further purification and isolation studies can be prepared by the Kline method...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1959
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.13-2127