Alan G. Castle

Royal College of Surgeons of England

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Neville Crawford

The Royal Free Hospital

Pál Gergely

University of Debrecen

R. Chibber

Royal College of Surgeons of England

N. Crawford

The Royal Free Hospital

COLIN LeGOOD

Royal College of Surgeons of England

Judith Marsh

King's College Hospital

Alvin C. Ling

National Tsing Hua University

Nyree Crawford

Almac (United Kingdom)

Cooperative Institutions

Royal College of Surgeons of England

The Honourable Society of Lincoln's Inn

The Royal Free Hospital

University College London

University of Oslo

University of Debrecen

Faculty (United Kingdom)

Hungarian Academy of Sciences

Institut de Chimie et Biochimie Moléculaires et Supramoléculaires

KU Leuven

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Isolation and Characterisation of Platelet “Tubulin”, a Sub-Unit Protein of the Microtubules

Thrombosis and Haemostasis (1975)

Nyree Crawford Alan G. Castle

From studies with whole platelets using microtubule binding agents such as colchicine and vinblastine, it appears that the microtubule have a cytoskeletal function and may be involved in shape changes, intracellular transport and other forms of cell motile activity. A microtubule subunit protein, “tubulin”, has been isolated from pig platelets and shown to have properties similar to tubulins from cilia, flagella and mammalian brains. The protein binds SH-colchicine, has a sedimentation constant as the dimer of about 6 S and the monomer (MW±55,000) coelectrophoreses with rat, rabbit and guineapig brain tubulins, running in acrylamide gels as a closely spaced doublet similar to the α and β components of brain tubulin. Some higher molecular weight presumptive dyrnein components are also present. The polymer formed during a temperature dependent “in vitri.)” assembly procedure has been studied by electron microscopy. Long linear aggregates with side to side association can be seen, resembling the microtubule subfilamentous structures seen in whole platelet preparations.

Colchicine

10.1055/s-0039-1689576

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Citations (1)

Absence of 5′-nucleotidase in porcine polymorphonuclear leucocyte membranes

Biochimica et Biophysica Acta (BBA) - Biomembranes (1982)

Alan G. Castle R. Chibber

5'-nucleotidase

Nucleotidase

10.1016/0005-2736(82)90374-1

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Citations (5)

Biochemical characterisation of porcine polymorphonuclear leucocytes: Comparison with human polymorphonuclear leucocytes

Comparative Biochemistry and Physiology Part B Comparative Biochemistry (1983)

R. Chibber Alan G. Castle

10.1016/0305-0491(83)90336-x

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Citations (7)

Phosphorylation of Platelet Microtubule Proteins by an Endogenous Protein Kinase

Biochemical Society Transactions (1976)

Alan G. Castle Neville Crawford

Conference Article| August 01 1976 Phosphorylation of Platelet Microtubule Proteins by an Endogenous Protein Kinase ALAN G. CASTLE; ALAN G. CASTLE 1Department of Biochemistry, University of Birmingham, P.O. Box 363, Birmingham B15 2TT, U.K. Search for other works by this author on: This Site PubMed Google Scholar NEVILLE CRAWFORD NEVILLE CRAWFORD 2Department of Biochemistry, University of Birmingham, P.O. Box 363, Birmingham B15 2TT, U.K. Search for other works by this author on: This Site PubMed Google Scholar Biochem Soc Trans (1976) 4 (4): 691–693. https://doi.org/10.1042/bst0040691 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn MailTo Cite Icon Cite Get Permissions Citation ALAN G. CASTLE, NEVILLE CRAWFORD; Phosphorylation of Platelet Microtubule Proteins by an Endogenous Protein Kinase. Biochem Soc Trans 1 August 1976; 4 (4): 691–693. doi: https://doi.org/10.1042/bst0040691 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Society Transactions Search Advanced Search This content is only available as a PDF. © 1976 Biochemical Society1976 Article PDF first page preview Close Modal You do not currently have access to this content.

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10.1042/bst0040691

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Citations (7)

Preparation of a Tubulin-Rich Protein Fraction from Pig Platelets

Biochemical Society Transactions (1975)

Alan G. Castle Neville Crawford

Conference Article| February 01 1975 Preparation of a Tubulin-Rich Protein Fraction from Pig Platelets ALAN G. CASTLE; ALAN G. CASTLE 1Department of Biochemistry, University of Birmingham, P.O. Box 363, Birmingham B15 2TT, U.K. Search for other works by this author on: This Site PubMed Google Scholar NEVILLE CRAWFORD NEVILLE CRAWFORD 1Department of Biochemistry, University of Birmingham, P.O. Box 363, Birmingham B15 2TT, U.K. Search for other works by this author on: This Site PubMed Google Scholar Biochem Soc Trans (1975) 3 (1): 164–166. https://doi.org/10.1042/bst0030164 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn MailTo Cite Icon Cite Get Permissions Citation ALAN G. CASTLE, NEVILLE CRAWFORD; Preparation of a Tubulin-Rich Protein Fraction from Pig Platelets. Biochem Soc Trans 1 February 1975; 3 (1): 164–166. doi: https://doi.org/10.1042/bst0030164 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Society Transactions Search Advanced Search This content is only available as a PDF. © 1975 Biochemical Society1975 Article PDF first page preview Close Modal You do not currently have access to this content.

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10.1042/bst0030164

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Citations (3)

Evidence against tubulin—actin homology

FEBS Letters (1976)

Alan G. Castle Judith Marsh Neville Crawford

Box Office

10.1016/0014-5793(76)80450-4

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Citations (3)

The binding of 125I-labeled concanavalin A to the cell surface of rabbit peritoneal polymorphonuclear leucocytes

Biochemical Medicine (1982)

Alan G. Castle COLIN LeGOOD

10.1016/0006-2944(82)90050-3

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Citations (5)

Isolation of tubulin from pig platelets

FEBS Letters (1975)

Alan G. Castle N. Crawford

Isolation

10.1016/0014-5793(75)80886-6

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Citations (17)

Purification and characterization of phosphorylase a from human platelets

International Journal of Biochemistry (1979)

Pál Gergely Alan G. Castle Neville Crawford

Dephosphorylation

Specific activity

Molecular mass

Sepharose

Phosphorylase kinase

10.1016/0020-711x(79)90053-3

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Citations (8)

Subcellular fractionation of porcine neutrophils by nitrogen cavitation and sucrose‐density‐gradient centrifugation

European Journal of Biochemistry (1983)

R. Chibber Alan G. Castle

Neutrophils, isolated in large quantities from porcine blood were disrupted by nitrogen cavitation and separated by differential centrifugation into a nuclear fraction and a post‐nuclear supernatant. The latter was subfractionated by sucrose density gradient centrifugation into cytosol, a fraction consisting of membrane vesicles and two granule‐rich fractions. The membrane fraction accounted for 1.9% of the protein in the post‐nuclear supernatant, the light granule fraction for 2.2% and the dense granule fraction for 4.2%. Catalase, lactate dehydrogenase and malate dehydrogenase were largely confined to the cytosol. The dense granule fraction contained the highest quantities of the hydrolytic enzymes, although the membrane fraction was also rich in alkaline and acid phosphatase and γ‐glutamyl transpeptidase activities. Electron microscopy of the membrane fraction showed intact membrane vesicles, whereas the granular fractions consisted of electron‐dense, membrane‐bound granules. Two granular fractions were isolated which contained granules of differing size and density. 3 H‐labeled wheat germ agglutinin bound to the surface of intact neutrophils and when these were disrupted and fractionated the membrane fraction showed a specific binding activity 16‐times greater than that of the cavitated sample. The membrane fraction interacted with the detergent digitonin and as a result underwent density perturbation increasing from 1.13 g . cm −3 to 1.18 g . cm −3 . Dodecylsulphate‐polyacrylamide gel electrophoresis showed the membrane fraction to consist of at least 40 protein bands, with relative molecular masses ranging from 200000–16000. The granule fractions contained less protein bands, with a protein composition quite distinct from that of the membrane fraction.

Sucrose gradient

Cell fractionation

Density gradient

Differential centrifugation

10.1111/j.1432-1033.1983.tb07753.x

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Citations (7)