Biomedical subjects

S S Twining

Publications and source records attributed to S S Twining.

57 records · Page 4Linked to original sources

PubMed1977

Identification of alpha1-acid glycoprotein, alpha2-macroglobulin and antithrombin III as components of normal and malignant human tissues.

alpha1-Acid glycoprotein, alpha2-macroglobulin, and antithrombin III have been identified, by immunological means, as components of the 90000 X g supernatant fraction of malignant and adjacent normal human breast, colon, and anal tissues, as well as malignant stomach and ileum. Malignant lung tissue only contained alpha1-acid glycoprotein. These protease inhibitors are immunologically equivalent to those present in human plasma.

Antithrombins↗

PubMed1977

Characterization of the interaction between chymotrypsin and heparin.

Heparin forms a complex with chymotrypsin which is active towards glutaryl-L-phenylalanine-p-nitroanilide (GPANA) and glutaryl-L-phenylalanine-beta-naphthylamide (GPNA) at pH 7.6. The activity of chymotrypsin towards GPANA at pH 7.6 is enhanced in the presence of heparin. Heparin does not bind at the active site of the enzyme since proflavin is not displaced from the active site of chymotrypsin upon complex formation. The heparin-chymotrypsin complex migrates under basic polyacrylamide disc gel electrophoresis conditions to a position intermediate between heparin and free chymotrypsin. The complex is dissociable under acidic polyacrylamide gel electrophoresis conditions. It is estimated that one to three molecules of heparin can bind to each chymotrypsin molecule on the basis of electrophoretic and enzymic activity data.

Binding Sites↗

PubMed1975

Isolation and identification of alpha1-antitrypsin as a component of normal and malignant human breast and other tissues.

Alpha1-Antitrypsin has been detected using radial immunodiffusion in the 90,000g supernatant fraction of malignant and adjacent normal human breast, colon, and anal tissue, as well as malignant lung, stomach, and ileum. Immobilized chymotrypsin, bound to Sepharose or Affi-Gel 10 has been utilized to separate 11 peaks of antiproteolytic activity by affinity chromatography of normal and malignant human breast tissue extracts. Glycoproteins are associated with eight of the peaks. Peak 1 contains predominantly alpha1-antitrypsin in addition to a minor component. The purification of the inhibitors, as judged by disc gel electrophoresis, is extensive. In some peaks, only one or two protein bands are observed, suggesting that affinity chromatography on Sepharose- or Affi-Gel 10-chymotrypsin might be used for the isolation of alpha1-antitrypsin and other inhibitors in preparative amounts.

Anal Canal↗