Gwent Reviews Its Needs
Gwent Education Authority systematically evaluates its policies, procedures, administration and the financial arrangements for young people with special educational needs. Julien Kramer, director of education, London Borough of Greenwich, until recently divisional director of education, School Support and Finance, Gwent, who has been working with service partners, the voluntary bodies and the district auditor, highlights strengths and weaknesses in service arrangements in Gwent and sets an agenda for change in anticipation of the requirements of the 1993 Education Act.
Special educational needs and the voluntary groups. A report on the consultative process
Abstract Derbyshire an English county authority, recently held a series of consultative meetings with the voluntary bodies and support organisations to review its educational arrangements for children and young people with special educational needs and to plan future provision. The consultative process is described and discussed. Issues emerging from the consultations are assessed against a background of current special educational needs developments in the education service and with regard to the changing nature of those English voluntary organisations representing the interests of young people with serious learning difficulties or serious disability.
Cytoplsmic uridine phosphorylase of rat liver. Characterization and kinetics.
Abstract Uridine phosphorylase (uridine:orthophosphate ribosyltransferase, EC 2.4.2.3) of rat liver cytoplasm has been purified 1900-fold. Initial velocity patterns of the phosphorolysis of uridine or deoxyuridine and of the synthesis of uridine indicated a sequential mechanism. Product inhibition patterns with uracil or ribose 1-phosphate as inhibitors were consistent with an "ordered Bi Bi" reaction in which inorganic phosphate is the first substrate to bind to the enzyme and ribose 1-phosphate the last product to leave the enzyme. The most highly purified enzyme fractions still retained uridine-, deoxyuridine-, and thymidine-cleaving activities in the ratio of 10:7:1 at pH 7.4. The fractions separated into a major and a minor band of protein on electrophoresis in phosphate buffer. Aging of the enzyme with loss of activity resulted in an increase in the proportion of the minor band. The pH optimum of the enzyme for uridine cleavage was 8.2, for deoxyuridine cleavage, 6.5, and for uridine synthesis, 8.5. Uridine or deoxyuridine synthesis was inhibited 50% in the presence of 1 mm uracil. The enzyme did not catalyze the direct transfer of ribose from uridine to uracil in the absence of phosphate. Uridine protected the enzyme to a greater degree than phosphate against inhibition by o-iodosobenzoate. Thus, at least one sulfhydryl group and possibly three are present at or near the active site. Uridine cleavage, uridine synthesis, and deoxyuridine cleavage were inhibited by deoxyglucosylthymine. The phosphorolysis of deoxyuridine and thymidine by thymidine phosphorylase, also purified from rat liver cytoplasm, was not inhibited by deoxyglucosylthymine. The molecular weights of both uridine and thymidine phosphorylases were estimated to be 110,000.