1. A specific collagenase from the culture medium of rabbit synovial fibroblasts was purified by gel filtration and ion-exchange chromatography. 2. The enzyme was homogeneous on polyacrylamide-gel electrophoresis and showed only traces of contaminants when tested in gels with a non-specific antiserum. 3. Therabbit fibroblast collagenase could hydrolyse collagen both in solution and in fibrillar...

Gelonin, a ribosome-inactivating protein has been isolated from the seeds of Gelonium multifluorum of Euphorbiaceae family by two methods and the results are compared. In method-I conventional aqueous extraction, cation-exchange and gel-filtration chromatography has been used. In method-II S-Sepharose fast flow gel has been used to purify the proteins from the seed extract, followed by ammonium...

An anomalous zymogram of lactate dehydrogenase (LDH) in the serum from a patient with liver cirrhosis was reported. Agar-gel electrophoresis of serum showed an extra LDH band close to the anodic side of LDH5 and a wide band of LDH5. Gel filtration of patient's serum in Sephadex G-200 demonstrated an abnormal LDH fraction eluted between immunoglobulin G (IgG) and macroglobulin in addition to a n...

Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) from Clostridium formicoaceticum has been purified to a specific activity of 469 mumol min-1 mg-1 at 35 degrees C, pH 7.2. The purified enzyme is homogeneous as judged by polyacrylamide disc gel electrophoresis, sedimentation velocity, and gel filtration profiles. The molecular weight is 41,000 +/- 200 as determined by sedimentation equilibri...

An aminopeptidase activity capable of hydrolyzing different aminomethylcoumarin amino acids, but mainly leucine-7-amino-4-methylcoumarin (Leu-NHMc), was detected in deoxycholic soluble extracts from adult Fasciola hepatica. The enzyme (EC 3.4.11.1) was partially purified by gel filtration and EAH-Sepharose affinity chromatography using bestatin as a ligand. Results obtained by gel filtration, d...

A thiamine-binding protein was purified from the extract of rice bran acetone powder by conventional procedures of acid precipitation, a series of column chromatography on DEAE-Sephadex A-50 and DEAE-cellulose, and gel filtration of Sephadex G-200. The purified thiamine-binding protein was nearly homogeneous as judged by disc gel electrophoresis and the molecular weight was estimated to be 94,0...

The plasma membrane-bound penicillinase of Bacillus licheniformis 749/C has been purified from bacteria grown in a medium containing [2-3H]glycerol and W-labeled aminoacids, and the purified enzyme compared with exopenicillinase. The procedure consisted of repeated chromatography on DEAE-Sephadex in the presence of Triton X-100, and gel filtration on Sephadex G-75 in the presence of taurodeoxyc...

The plasma membrane-bound penicillinase of Bacillus licheniformis 749/C has been purified from bacteria grown in a medium containing [2-3H]glycerol and W-labeled aminoacids, and the purified enzyme compared with exopenicillinase. The procedure consisted of repeated chromatography on DEAE-Sephadex in the presence of Triton X-100, and gel filtration on Sephadex G-75 in the presence of taurodeoxyc...

Nitrate reductase, released from the membrane fraction of Escherichia coli by a neutral heat treatment, was purified to homogeneity by gel filtration chromatography. The purified enzyme behaved as an associating-dissociating system, exhibiting concentration-dependent sedimentation constants which ranged from 24 S at high concentrations in the ultracentrifuge down to 10 S at low concentrations i...