Biomaterial Database

Purification fo cathepsin D by AH-sepharose affinity chromatography. 1978

A Linde, and B Persliden

A rapid and reliable method for coupling the protease inhibitor pepstatin to AH-Sepharose 48 was developed. The matrix prepared was used to purify cathepsin D from rat liver. The enzyme was eluted in one fraction and proved to be pure by gel electrophoresis, two types of ion exchange chromatography, molecular sieve chromatography, and immunologically homogenous by immunoelectrophoresis. This method is more rapid and gives a higher yield than previous techniques. The possibility to use this technique for the purification of other enzymes inhibitable by pepstatin should be considered.

UI	MeSH Term	Description	Entries
D008722	Methods	A series of steps taken in order to conduct research.	Techniques,Methodological Studies,Methodological Study,Procedures,Studies, Methodological,Study, Methodological,Method,Procedure,Technique
D002403	Cathepsins	A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.	Cathepsin
D002846	Chromatography, Affinity	A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D012685	Sepharose		Agarose,Sepharose 4B,Sepharose C1 4B,4B, Sepharose C1,C1 4B, Sepharose