Search Results - "Derham, Barry K."

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  1. 1

    The mechanism of inactivation of glucose oxidase from Penicillium amagasakiense under ambient storage conditions by Caves, Michael S., Derham, Barry K., Jezek, Jan, Freedman, Robert B.

    Published in Enzyme and microbial technology (10-06-2011)
    “…Glucose oxidase (GOx) from Penicillium amagasakiense has a higher specific activity than the more commonly studied Aspergillus niger enzyme, and may therefore…”
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    Journal Article
  2. 2

    Biopharmaceutical formulations for pre-filled delivery devices by Jezek, Jan, Darton, Nicholas J, Derham, Barry K, Royle, Nikki, Simpson, Iain

    Published in Expert opinion on drug delivery (01-06-2013)
    “…Pre-filled syringes are becoming an increasingly popular format for delivering biotherapeutics conveniently and cost effectively. The device design and stable…”
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  3. 3

    Thermal Inactivation of Uricase (Urate Oxidase): Mechanism and Effects of Additives by Caves, Michael S, Derham, Barry K, Jezek, Jan, Freedman, Robert B

    Published in Biochemistry (Easton) (22-01-2013)
    “…Uricase (Urc) is an oxidoreductase enzyme of both general and commercial interest, the former because of its lack of a cofactor and the latter because of its…”
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  4. 4

    The effect of the presence of globular proteins and elongated polymers on enzyme activity by Derham, Barry K., Harding, John J.

    Published in Biochimica et biophysica acta (01-06-2006)
    “…We have studied the effect of a crowded (macromolecular) solution on reaction rates of the decarboxylating enzymes urease, pyruvate decarboxylase and glutamate…”
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  5. 5

    α-Crystallin as a molecular chaperone by Derham, Barry K, Harding, John J

    Published in Progress in retinal and eye research (01-07-1999)
    “…The role of α-crystallin as a molecular chaperone may explain how the lens stays transparent for so long. α-Crystallin prevents the aggregation of other lens…”
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  6. 6

    Effects of modifications of alpha-crystallin on its chaperone and other properties by Derham, Barry K, Harding, John J

    Published in Biochemical journal (15-06-2002)
    “…The role of alpha-crystallin, a small heat-shock protein and chaperone, may explain how the lens stays transparent for so long. alpha-Crystallin prevents the…”
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  7. 7

    Enzyme activity after resealing within ghost erythrocyte cells, and protection by alpha-crystallin against fructose-induced inactivation by Derham, Barry K, Harding, John J

    Published in Biochemical journal (15-12-2002)
    “…The role of alpha-crystallin as a molecular chaperone has been shown in many in vitro studies. In the present paper, we report on the chaperone function of…”
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  8. 8

    Effect of aging on the chaperone-like function of human alpha-crystallin assessed by three methods by Derham, B K, Harding, J J

    Published in Biochemical journal (15-12-1997)
    “…alpha-Crystallin can function as a molecular chaperone by preventing unwanted interactions. This paper presents the effects of aging and cataract on the…”
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  9. 9

    The molecular chaperone α‐crystallin incorporated into red cell ghosts protects membrane Na/K‐ATPase against glycation and oxidative stress by Derham, Barry K., Ellory, J. Clive, Bron, Anthony J., Harding, John J.

    Published in European journal of biochemistry (01-06-2003)
    “…α‐Crystallin, a molecular chaperone and lens structural protein protects soluble enzymes against heat‐induced aggregation and inactivation by a variety of…”
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  10. 10

    The effects of ageing on the chaperone-like function of rabbit α-crystallin, comparing three methods of assay by Derham, Barry K, Harding, John J

    Published in Biochimica et biophysica acta (29-08-1997)
    “…The lens has a high protein content necessary for focusing light on to the retina. α-Crystallin accounts for approximately 40% of the protein and has been…”
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  11. 11
  12. 12

    Identification of cell markers of the nucleus and annulus of bovine intervertebral discs by Derham, Barry K., Urban, Jill

    “…Introduction  The intervertebral disc consists of three regions, the nucleus pulpous and the inner and outer annulus containing cells with individual…”
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  13. 13

    Chaperone function of mutant versions of αA‐ and αB‐crystallin prepared to pinpoint chaperone binding sites by Derham, Barry K., van Boekel, Martinus A. M., Muchowski, Paul J., Clark, John I., Horwitz, Joseph, Hepburne‐Scott, Henry W., de Jong, W. W., Crabbe, M. James C., Harding, John J.

    Published in European journal of biochemistry (01-02-2001)
    “…A major stress protein, α‐crystallin, functions as a chaperone. Site‐directed mutagenesis has been used to identify regions of the protein necessary for…”
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