Biography:

One of their most recent publications is The isolation and characterization of deoxyribonucleoproteins from human spleen. Which was published in journal Archives of Biochemistry and Biophysics.

More information about John R. Kongsvik research including statistics on their citations can be found on their Copernicus Academic profile page.

John R. Kongsvik's Articles: (5)

The isolation and characterization of deoxyribonucleoproteins from human spleen

AbstractThe extraction and characterization of deoxyribonucleoproteins (DNP) from the purified nuclei of human spleen with 0.01 m glycine solution is described. The glycine extract was found to consist of a DNA-protein complex containing 29% DNA and 71% protein. The DNA was undegraded, highly fibrous, and of the “A-T” type. The protein moiety of the DNP had an amino acid composition characteristic of histones. When the DNP was tested by cellulose acetate electrophoresis in low ionic strength buffer it moved toward the anode as a single band. Similarly, the elution of the DNP from Sephadex G-25, G-50, and, most significantly, G-200 columns resulted in the recovery of a single peak containing both DNA and protein. When injected into rabbits, the DNP was antigenic and gave a single, sharp precipitin line when tested against antispleen DNP serum.

The isolation and characterization of deoxyribonucleoproteins from human spleen

AbstractThe extraction and characterization of deoxyribonucleoproteins (DNP) from the purified nuclei of human spleen with 0.01 m glycine solution is described. The glycine extract was found to consist of a DNA-protein complex containing 29% DNA and 71% protein. The DNA was undegraded, highly fibrous, and of the “A-T” type. The protein moiety of the DNP had an amino acid composition characteristic of histones. When the DNP was tested by cellulose acetate electrophoresis in low ionic strength buffer it moved toward the anode as a single band. Similarly, the elution of the DNP from Sephadex G-25, G-50, and, most significantly, G-200 columns resulted in the recovery of a single peak containing both DNA and protein. When injected into rabbits, the DNP was antigenic and gave a single, sharp precipitin line when tested against antispleen DNP serum.

The isolation and characterization of deoxyribonucleoproteins from human spleen

AbstractThe extraction and characterization of deoxyribonucleoproteins (DNP) from the purified nuclei of human spleen with 0.01 m glycine solution is described. The glycine extract was found to consist of a DNA-protein complex containing 29% DNA and 71% protein. The DNA was undegraded, highly fibrous, and of the “A-T” type. The protein moiety of the DNP had an amino acid composition characteristic of histones. When the DNP was tested by cellulose acetate electrophoresis in low ionic strength buffer it moved toward the anode as a single band. Similarly, the elution of the DNP from Sephadex G-25, G-50, and, most significantly, G-200 columns resulted in the recovery of a single peak containing both DNA and protein. When injected into rabbits, the DNP was antigenic and gave a single, sharp precipitin line when tested against antispleen DNP serum.

The isolation and characterization of deoxyribonucleoproteins from human spleen

AbstractThe extraction and characterization of deoxyribonucleoproteins (DNP) from the purified nuclei of human spleen with 0.01 m glycine solution is described. The glycine extract was found to consist of a DNA-protein complex containing 29% DNA and 71% protein. The DNA was undegraded, highly fibrous, and of the “A-T” type. The protein moiety of the DNP had an amino acid composition characteristic of histones. When the DNP was tested by cellulose acetate electrophoresis in low ionic strength buffer it moved toward the anode as a single band. Similarly, the elution of the DNP from Sephadex G-25, G-50, and, most significantly, G-200 columns resulted in the recovery of a single peak containing both DNA and protein. When injected into rabbits, the DNP was antigenic and gave a single, sharp precipitin line when tested against antispleen DNP serum.

Short communicationSubfractionation of CsCI-purified H-1 parvovirus on metrizamide gradients

AbstractThe different density classes of H-1 parvovirus, collected within 30 hr of parection of parasynchronous cultures, following the standard CsCl purification step, have been shown to be heterogeneous. Rebanding of the denser form (HF, ϱ = 1.46 g/cm3) and the less dense form (LF, ϱ = 1.42 g/cm3) of infectious virus in the nonionic density generating solute, metrizamide, showed that both HF and LF virus bands were heterogeneous in density. The infectivity banded with isotopically labeled virus protein and DNA at 1.32 g/cm3 for both HF and LF virus. Amounts of protein and DNA which varied from preparation to preparation, but which were greater from the HF virus band, were distributed throughout the rest of the gradient, but predominated in a peak at a density of 1.2 g/cm3. The protein in this peak was without hemagglutinating activity but had the molecular weights and proportions of the H-1 virion proteins (VP1, VP2′, and VP2). The DNA was of the same size as H-1 DNA monomers and its proportion to the protein was similar to that of the infectious peak. The DNA was susceptible to micrococcal nuclease digestion. The nature of this noninfectious viral material thus seemed to be incompletely assembled virus. Radio-labeled H-1 virus collected after 72 hr of infection formed a discrete single peak in both CsCl (ϱ = 1.42 g/cm3), and metrizamide gradients (ϱ = 1.32 g/cm3). There was no significant amount of the 1.20 g/cm3 viral protein-DNA complex in these mature preparations.

Advertisement
Join Copernicus Academic and get access to over 12 million papers authored by 7+ million academics.
Join for free!

Contact us