Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.22.32 (bromelain)
 1,025 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Multiforms of aminopeptidases and arylamidases in normal human liver, stomach, lung, ileum, colon, rectum, and kidney, and cancer tissue from human liver, stomach, and lung were separated by triethylaminoethyl cellulose column chromatography. The aminopeptidases and arylamidases were solubilized from human tissues by treatment with bromelain, and their column chromatograms on triethylaminoethyl-cellulose gave different patterns of multiforms of enzymes in these tissues. The fractions of enzymes separated specificities toward L-leucyl-beta-naphthylamide, L-leucinamide, L-methioninamide, L-phenylalaninamide, and L-alaninamide. The activity of aminopeptidase toward L-leucinamide and of arylamidase toward L-leucyl-beta-naphthylamide was higher in human stomach cancer tissue and lower in hepatic cancer tissue than in normal stomach and liver, respectively. In lung cancer tissue, the activity of aminopeptidase toward L-leucinamide was abnormally low, while the activity of arylamidase toward L-leucyl-beta-napthylamide was similar to that in normal lung. The substrate specificities or patterns of the multiforms of these enzymes in cancer tissue from human liver, stomach, and lung were shown to differ from those of normal liver, stomach, and lung, respectively, by triethylaminoethyl cellulose column chromatography.
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PMID:Aminopeptidases and arylamidases in normal and cancer tissues in humans. 111 41

Arylamidase (E.C. 3.4.11.2) was solubilized from renal cancer tissues by bromelain treatment, and its properties were compared with those of normal kidney and placental enzymes after partial purification. Their column chromatograms on TEAE-cellulose revealed a slight, but constant difference in the negative charge, namely, in normal kidney, renal cancer tissue, and placental enzymes in increasing order. An electrophoretic study on polyacrylamide gel showed comparable results. On the other hand, when treated with neuraminidase prior to electrophoresis, the renal cancer tissue and kidney enzymes came to have an identical mobility, while the placental enzyme still had a faster mobility than the others. The renal cancer tissue arylamidase was not clearly distinguished from the kidney and placental enzymes with respect to molecular weight, Michaelis constant, pH optimum, heat stability, behavior to divalent cations or chelating agents, susceptibility to urea or amino acids, inhibition by sulfhydryl agents, and immunological properties. These results suggest that renal cancer tissue and kidney enzymes are similar glycoproteins, simply different in sialic acid content, and that these two enzymes are different from the placental enzyme in the structure of the peptide portion and/or carbohydrate portions other than sialic acid residues.
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PMID:Arylamidase from human renal cancer tissue in comparison with normal kidney and placental enzymes. 679 1