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3.4.23.5: cathepsin D

This is an abbreviated version!
For detailed information about cathepsin D, go to the full flat file.

Word Map on EC 3.4.23.5

Reaction

Specificity similar to, but narrower than, that of pepsin A. Does not cleave the Gln4-His bond in B chain of insulin =

Synonyms

BmCatD, CAD 1, CAD 2, CAD 3, CapD, Cat D, CAT-D, CatD, Cath D, cath-D, cathD, cathepsin D, cathepsin D-like proteinase, cathepsin D1, cathepsin D2, CD1, CTSD, EC 3.4.4.23, matCTSD, PCD, Pep4p, preproCatD, pro-cathepsin, pro-cathepsin D, pro-CD, pro-CtsD, proCat, proCDrec, proCTSD, Proteinase A

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.5 cathepsin D

Purification

Purification on EC 3.4.23.5 - cathepsin D

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3 cathepsin D components: Cath-D-I, Cath D-II, and Cath D-III
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3 major forms of enzyme: alpha, beta, gamma
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affinity purification, 2 enzyme forms, the major form is termed cathepsin D-1, the minor form is termed cathepsin D-II
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ammonium sulfate precipitation and pepstatin A affinity gel filtration
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ammonium sulfate precipitation, Sephadex G-100 gel filtration, Mono-S column chromatography, Sephadex G-75 gel filtration, and Mono-S column chromatography
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ANTI-FLAG M2 affinity resin column chromatography, and gel filtration
glutathione Sepharose column chromatography
isoenzyme A and B
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Ni2+-Sepharose column chromatography
partial purification by ultrafiltration and pepstatin agarose resin chromatography
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pepstatin A affinity column chromatography
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pepstatin A agarose column chromatography
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pepstatin A agarose gel column chromatography
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pepstatin A-agarose column chromatography and centrifugal filtration
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pepstatin A-agarose column chromatography, NAP-5 Sephadex G25 gel filtration, and UNO Q1 column chromatography
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pepstatin-A affinity chromatography
purified by ammonium sulfate precipitation and octyl sepharose, Con-A sepharose, CM-sephadex columns sequentially. Finally, by preparative gel electrophoresis. On SDS-PAGE the purified preparation gives two bands 50 kDa and 47 kDa. The upper band is characterized as cathepsin D and the lower band as sialidase. The two enzymes are separated from each other by using high-performance gel-filtration chromatography
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purified from a bovine brain homogenate
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recombinant CAD 3 is purified by HisTrap column chromatography
six isoenzymes, large scale purification
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using Pepstatin A-affinity purification
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using pepstatin A-chromatography
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