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Biomedical subjects

J S Hansen

Publications and source records attributed to J S Hansen.

At least 37 records · Page 2Linked to original sources
PubMed1982

Identification of tumor-associated antigens on ultraviolet light-induced tumors using antitumor antibodies developed in ascites fluid.

A method is described which leads to the production of large amounts of ascites containing antitumor antibody in small numbers of mice. The antibody was then used to identify and characterize tumor-associated antigens on an ultraviolet light-induced murine skin fibrosarcoma. The antibody showed specific complement-dependent cytotoxicity to the homologous tumor and to an allogeneic tumor line which displayed a glycoprotein viral determinant with a molecular weight of 70,000 on its surface. Absorption of the immune ascites with other tumor cell lines removed the cytotoxicity in relation to the presence of the glycoprotein. Isolation of the tumor cell surface components binding antibody revealed two components with molecular weights of approximately 70,000 and 60,000. The Mr 70,000 component was identified as viral gp70 by peptide mapping.

Animals↗
PubMed1982

Intermolecular disulfide bonding of lens membrane proteins during human cataractogenesis.

Two-dimensional diagonal electrophoresis has been used to characterize intermolecular disulfide bonding of membrane proteins from lenses of cataractous and normal patients. A component of approximately 18,000 daltons, linked via intermolecular disulfide bonding, was found in membrane preparations from 10 of 17 cataracts studied. In comparison, membrane from only 1 of 12 normal lenses of approximately the same age range was found to contain intermolecular disulfide bonding of a component of similar molecular weight. Treatment of normal lens with the oxidizing agents cupric sulfate and 1,10-phenanthroline resulted in intermolecular disulfide bonding of the 18K component in a manner similar to that found in cataractous lenses. Together these results demonstrate that human cataractogenesis is many times accompanied by intermolecular disulfide bonding of a membrane component of 18K and suggest that this intermolecular bonding may be the result of the previously reported oxidative insult of the lens during human cataract formation.

Adult↗
PubMedDate not supplied

Biochemical analysis of microdissected sections from the normal and cataractous human lens.

To better compare possible changes in soluble protein content during human cataractogenesis, microdissected sections from opaque and highly pigmented versus transparent parts of the lens were analyzed by high pressure liquid chromatography, isoelectric focusing, sodium dodecylsulfate polyacrylamide gel electrophoresis, and tryptic mapping of radioiodinated peptides. Using this methodology, resolution of proteins and their tryptic peptides can be obtained from individual lens sections containing as little as 5-10 micrograms of protein. Furthermore, the origin of each protein analyzed by these methods can be verified by comparison with tryptic peptide maps of previously purified human crystallins. Included are examples of how this technique can be used to characterize differences in protein composition from opaque versus transparent sections from different human lenses, as well as brunescent vs lightly-pigmented sections from the same human lens.

Autoradiography↗