A comparison of four sulfhydryl cathepsins (B, C, H, and L) from porcine spleen

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Abstract
Four sulfhydryl cathepsins, B, C (dipeptidylaminopeptidase I), H and L were isolated from porcine spleen. They are all glycoproteins of similar amino acid compositions, which are comparable with those of cathepsins B and H from other sources and so with papain. All 4 cathepsins exist in multiple charged forms: B, C, H and L have isoelectric points in the range 4.3-5.4, 5.3 and 5.9, 5.2-5.7 and 7-8.7, respectively. The MW of cathepsins B and H were 24,000 and 26,000. Anomalous behavior of cathepsin L on both conventional gel filtration and high pressure liquid chromatography precluded a precise assessment of its MW which is between 22,000 and 28,000. The isolated mercurial derivative of cathepsin C has a MW of 56,000 (an active dimer formed on reduction). Cathepsins B and H also aggregate.