Zobrazeno 1 - 5
of 5
pro vyhledávání: '"F. A. O. Marston"'
Publikováno v:
The Biochemical journal. 271(2)
1. Prochymosin in solution in the presence of 8 M-urea is fully unfolded, as indicated by its fluorescence spectrum, fluorescence quenching behaviour and far-u.v.c.d. spectrum. 2. Equilibrium studies on the unfolding of prochymosin and pepsinogen by
Autor:
Peter A. Koklitis, A.F. Carne, Sarojani Angal, Robert B. Freedman, Harris T J R, Bryan J. Smith, Maria Panico, Howard R. Morris, F. A. O. Marston, Richard A. Williamson
Publikováno v:
The Biochemical journal. 268(2)
Disulphide bonds in human recombinant tissue inhibitor of metalloproteinases (TIMP) were assigned by resolving proteolytic digests of TIMP on reverse-phase h.p.l.c. and sequencing those peaks judged to contain disulphide bonds by virtue of a change i
Autor:
F. A. O. Marston, Sarojani Angal, Peter A. Lowe, Susan White, Michael T. Doel, Joyce M. Schoemaker
Publikováno v:
Nature Biotechnology. 2:800-804
Recombinant calf prochymosin synthesized in E. coli was shown to accumulate in the form of insoluble inclusion bodies. Isolation of this aggregated material, combined with specific washing procedures, was the most significant stage of the purificatio
Publikováno v:
Nature Biotechnology. 4:553-557
The size distribution and density of two types of protein inclusion bodies arising from the synthesis in E. coli of recombinant calf prochymosin and γ–interferon were examined. A combination of electrical sensing zone and centrifugal sedimentation
Publikováno v:
The EMBO journal. 4(3)
Recent reports have shown that synthesis of certain recombinant proteins in Escherichia coli results in the production of intracellular inclusion bodies. These studies have not analyzed the structure of the inclusion body especially regarding the int