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FRANK B. WILLIAMSON
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120 Heparinase-II-catalysed degradation of N -propionylated heparin

Colin F. Moffat, William F. Long, Maitland W. McLean, Frank B. Williamson
Biochem Soc Trans (1997) 25 (4): S654.
DOI: https://doi.org/10.1042/bst025s654
Published: 01 November 1997
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The antioxidant activity of heparins

DAVID GRANT, WILLIAM F. LONG, GILLIAN MACKINTOSH, FRANK B. WILLIAMSON
Biochem Soc Trans (1996) 24 (2): 194S.
DOI: https://doi.org/10.1042/bst024194s
Published: 01 May 1996
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Similarity and dissimilarity in aspects of the binding to heparin of Ca 2+ and Zn 2+ as revealed by Potentiometrie titration

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1996) 24 (2): 203S.
DOI: https://doi.org/10.1042/bst024203s
Published: 01 May 1996
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The binding of platinum (II) to heparin

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1996) 24 (2): 204S.
DOI: https://doi.org/10.1042/bst024204s
Published: 01 May 1996
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Evidence from potentiometric titration for lack of reversibility in the interaction between heparin and Cu 2+ or Ca 2+ ions

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (4): 362S.
DOI: https://doi.org/10.1042/bst020362s
Published: 01 November 1992
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The effect of heparin on the u.v. absorption properties of Fe(II) and Fe(III)

MAIRI F. WILLIAMSON, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (4): 360S.
DOI: https://doi.org/10.1042/bst020360s
Published: 01 November 1992
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Complexation of Fe 2+ ions by heparin

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (4): 361S.
DOI: https://doi.org/10.1042/bst020361s
Published: 01 November 1992
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Complexation of Zn 2+ ions by heparin

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (4): 363S.
DOI: https://doi.org/10.1042/bst020363s
Published: 01 November 1992
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Heparin inhibits production of thiobarbituric acid-reactive substances in the the presence of linolenic acid and Fe 2+ ions

MARION A. ROSS, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (4): 364S.
DOI: https://doi.org/10.1042/bst020364s
Published: 01 November 1992
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13 C-n.m.r. spectroscopy of Cu 2+ -heparin suggests phase separation of the complex from Cu 2+ in aqueous solution

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (2): 214S.
DOI: https://doi.org/10.1042/bst020214s
Published: 01 May 1992
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Examination of cation-heparin interaction by potentiometric titration

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (2): 215S.
DOI: https://doi.org/10.1042/bst020215s
Published: 01 May 1992
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Effect of chemically modified heparins, and of heparin fragments, on Fe(II)-catalyzed peroxidation of linolenic acid

MARION A. ROSS, WILLIAM F. LONG, FRANK B. WILLIAMSON, COLIN F. MOFFAT
Biochem Soc Trans (1992) 20 (2): 216S.
DOI: https://doi.org/10.1042/bst020216s
Published: 01 May 1992
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The effect of Cu(II) ions on the optical rotation of heparin

DAVID GRANT, WILLIAM F. LONG, COLIN F. MOFFAT, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (1): 1S.
DOI: https://doi.org/10.1042/bst020001s
Published: 01 February 1992
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Heparin reduces Fe(II)-catalyzed peroxidation of linolenic acid

MARION A. ROSS, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (1): 6S.
DOI: https://doi.org/10.1042/bst020006s
Published: 01 February 1992
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Polarimetry of mixtures of Cu(II) ions and chemically modified heparins

DAVID GRANT, WILLIAM F. LONG, COLIN F. MOFFAT, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (1): 2S.
DOI: https://doi.org/10.1042/bst020002s
Published: 01 February 1992
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Decrease in carboxylate absorption during heparin-poly L -lysine interaction

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (1): 3S.
DOI: https://doi.org/10.1042/bst020003s
Published: 01 February 1992
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Multiple-specular-reflectance i.r. spectroscopy of glycosaminoglycan-cetylpyridinium complexes

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1992) 20 (1): 4S.
DOI: https://doi.org/10.1042/bst020004s
Published: 01 February 1992
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N.m.r. spectroscopy of Ca 2+ -heparin suggests delocalized binding of the cation

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1991) 19 (4): 390S.
DOI: https://doi.org/10.1042/bst019390s
Published: 01 November 1991
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Ca 2+ -heparin interaction investigated polarimetrically

DAVID GRANT, COLIN F. MOFFAT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1991) 19 (4): 391S.
DOI: https://doi.org/10.1042/bst019391s
Published: 01 November 1991
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A relationship between cation-induced changes in heparin optical rotation and heparin-cation association constants

DAVID GRANT, COLIN F. MOFFAT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1991) 19 (4): 392S.
DOI: https://doi.org/10.1042/bst019392s
Published: 01 November 1991
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Optical rotation changes in chemically modified heparins as a guide to anionic groups involved in Ca 2+ binding

DAVID GRANT, COLIN F. MOFFAT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1991) 19 (4): 393S.
DOI: https://doi.org/10.1042/bst019393s
Published: 01 November 1991
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Carboxylate symmetric stretching frequencies and optical rotation shifts of heparin-cation complexes

DAVID GRANT, COLIN F. MOFFAT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1991) 19 (4): 394S.
DOI: https://doi.org/10.1042/bst019394s
Published: 01 November 1991
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I.r. spectroscopic analysis of heparin-polypeptide interaction

DAVID GRANT, WILLIAM F. LONG, FRANK. B. WILLIAMSON
Biochem Soc Trans (1991) 19 (4): 395S.
DOI: https://doi.org/10.1042/bst019395s
Published: 01 November 1991
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Infrared spectroscopy as a method for investigating the conformations of iduronate saccharide residues in glycosaminoglycans

DAVID GRANT, WILLIAM F. LONG, COLIN F. MOFFAT, FRANK B. WILLIAMSON
Biochem Soc Trans (1990) 18 (6): 1277-1279.
DOI: https://doi.org/10.1042/bst0181277a
Published: 01 December 1990
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Effect of chemical reduction of the iduronate of heparin on i.r. absorption bands sensitive to sugar conformation

DAVID GRANT, WILLIAM F. LONG, COLIN F. MOFFAT, FRANK B. WILLIAMSON
Biochem Soc Trans (1990) 18 (6): 1279-1280.
DOI: https://doi.org/10.1042/bst0181279
Published: 01 December 1990
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A possible ring conformational change of iduronate residues detected by i.r. spectroscopy of aqueous solutions of lithium-heparin

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1990) 18 (6): 1281-1282.
DOI: https://doi.org/10.1042/bst0181281
Published: 01 December 1990
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Iduronate residue ring conformations in heparan sulphates of normal and transformed fibroblasts

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1990) 18 (6): 1282-1283.
DOI: https://doi.org/10.1042/bst0181282
Published: 01 December 1990
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The dependence on counter-cation of the degree of hydration of heparin

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1990) 18 (6): 1283-1284.
DOI: https://doi.org/10.1042/bst0181283
Published: 01 December 1990
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Carboxylate symmetric stretching infrared absorbances of chemically modified heparins

DAVID GRANT, COLIN F. MOFFAT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1989) 17 (3): 500-501.
DOI: https://doi.org/10.1042/bst0170500
Published: 01 June 1989
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N -Acetyl amide-II and methyl C—H bending infrared absorbances of chemically modified heparins

DAVID GRANT, COLIN F. MOFFAT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1989) 17 (3): 502-503.
DOI: https://doi.org/10.1042/bst0170502
Published: 01 June 1989
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N -Sulphonate infrared absorbances of chemically modified heparins

DAVID GRANT, COLIN F. MOFFAT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1989) 17 (3): 498-500.
DOI: https://doi.org/10.1042/bst0170498
Published: 01 June 1989
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Heparans as pericellular antioxidants

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1988) 16 (6): 977-978.
DOI: https://doi.org/10.1042/bst0160977
Published: 01 December 1988
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A model of Ca 2+ -heparin interaction

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1988) 16 (6): 1028-1029.
DOI: https://doi.org/10.1042/bst0161028
Published: 01 December 1988
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Polystyrene surfaces may require structured water for effective cell adhesion

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1988) 16 (6): 1029-1030.
DOI: https://doi.org/10.1042/bst0161029
Published: 01 December 1988
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Effect of heparin on dismutation of superoxide ions

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1988) 16 (6): 1030-1031.
DOI: https://doi.org/10.1042/bst0161030
Published: 01 December 1988
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Juxtaposition of particular amino acid residues may contribute to the protection of proteins from active free radicals

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1987) 15 (6): 1098.
DOI: https://doi.org/10.1042/bst0151098
Published: 01 December 1987
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Analysis of heparin N -sulphonate absorbancies interpreted in terms of two polymer conformations

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1987) 15 (6): 1087-1088.
DOI: https://doi.org/10.1042/bst0151087
Published: 01 December 1987
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Incorporation of 35 S into glycosaminoglycans of ovarian follicular granulosa cells

WILLIAM F. LONG, MICHAEL CLINTON, FRANK B. WILLIAMSON, J. S. MORLEY HUTCHINSON, BARRIE SEDDON
Biochem Soc Trans (1985) 13 (2): 388-389.
DOI: https://doi.org/10.1042/bst0130388
Published: 01 April 1985
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A role for glycosaminoglycans in cellular adhesion of relevance to the cancer state

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1985) 13 (2): 389.
DOI: https://doi.org/10.1042/bst0130389
Published: 01 April 1985
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Histidine-rich glycoprotein alleviates the inhibition by heparin of thrombin-induced platelet aggregation

GEORGE KINDNESS, E. ANNE VIGROW, WILLIAM F. LONG, FRANK B. WILLIAMSON, WILLIAM T. MORGAN, JENG CHANG
Biochem Soc Trans (1984) 12 (5): 846-847.
DOI: https://doi.org/10.1042/bst0120846
Published: 01 October 1984
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Polarimetry as a technique for the study of glycosaminoglycan-metal-ion interactions

COLIN F. MOFFAT, DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1984) 12 (2): 301.
DOI: https://doi.org/10.1042/bst0120301
Published: 01 April 1984
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Altered water structure in mixtures of heparin and metal ions

DAVID GRANT, COLIN F. MOFFAT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1984) 12 (2): 302.
DOI: https://doi.org/10.1042/bst0120302
Published: 01 April 1984
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Amidolytic activity of 7S nerve growth factor

WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1984) 12 (2): 244-246.
DOI: https://doi.org/10.1042/bst0120244
Published: 01 April 1984
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Heparan sulphates of chemically transformed BHK cells in which the transformed growth trait is temperature-dependent

NANCY E. WOODHEAD, WILLIAM F. LONG, FRANK B. WILLIAMSON, WILLIAM J. HARRIS
Biochem Soc Trans (1984) 12 (2): 300-301.
DOI: https://doi.org/10.1042/bst0120300
Published: 01 April 1984
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Zinc ion binding by heparin

NANCY E. WOODHEAD, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1983) 11 (1): 96-97.
DOI: https://doi.org/10.1042/bst0110096a
Published: 01 January 1983
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Effect of heparin molecular-size fractions on the inhibition of proteinases by antithrombin III

WILLIAM F. LONG, FRANK B. WILLIAMSON, NANCY E. WOODHEAD
Biochem Soc Trans (1983) 11 (1): 97-98.
DOI: https://doi.org/10.1042/bst0110097
Published: 01 January 1983
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Analysis by infrared spectroscopy of the association of water and metal ions with heparin

DAVID GRANT, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1983) 11 (1): 96.
DOI: https://doi.org/10.1042/bst0110096
Published: 01 January 1983
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The heparan sulphates of normal and virus-transformed hamster fibroblasts

NANCY E. WOODHEAD, WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1981) 9 (6): 555-556.
DOI: https://doi.org/10.1042/bst0090555
Published: 01 December 1981
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Effect of heparin on the inhibition by α 1 -proteinase inhibitor of amidolysis catalysed by thrombin, factor X a and plasmin

WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1981) 9 (5): 408.
DOI: https://doi.org/10.1042/bst0090408
Published: 01 October 1981
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Effect of dithiothreitol on the modulation of antithrombin III activity by sulphated polysaccharides

WILLIAM F. LONG, FRANK B. WILLIAMSON
Biochem Soc Trans (1981) 9 (1): 68-69.
DOI: https://doi.org/10.1042/bst0090068
Published: 01 February 1981
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