The proteins removed from the extracellular space of dark‐grown pea (Pisum sativum L. cv. Alaska) internode sections by centrifugation were studied. A large number of proteins were resolved by sodium dodecyl sulfate polyacrylamide gel electrophoresis. These proteins ranged in size from 10 to 150 kdalton and their removal from the cell wall was greatly facilitated by the presence of salts of divalent and trivalent cations in the infiltration medium. Pulse‐labelling experiments with [35S)‐methionine showed that many of the proteins extracted from the cell wall incorporated radioactivity and that treatment with indoleacetic acid (IAA) altered the pattern of radiolabel incorporation. One of the proteins centrifuged from pea internode sections possessed per‐oxidase (EC 1.11.1.7) activity. The activity of this peroxidase increased less in auxin‐treated internode segments than in untreated controls. Antibodies were raised to the total protein fraction extracted by centrifugation and used to localize antigens on protein blots. Most of the proteins centrifuged from pea internode sections were stained by a dye coupled to the cell wall antiserum. Light microscopic immunohistochemical studies showed that the proteins centrifuged from dark‐grown pea internodes were localized almost exclusively in the cell wall and intercellular spaces of pea internode tissue. Light microscopic immunohistochemistry also showed that antibodies to extracted proteins penetrate into the apoplast of abraded pea internode segments and split pea stems. These antibodies did not influence growth of IAA‐treated or control tissue.
The commercial development of advanced therapy medicinal products (ATMPs) represents great opportunity for therapeutic innovation but is beset by many challenges for its developers. Although the ATMP field continues to progress at a rapid pace, evidenced by the increasing number of clinical trials conducted over the past few years, several factors continue to complicate the introduction of ATMPs as a curative treatment for multiple disease types, by blocking their translational pathway from research to the patient. While several recent publications (Trounson and McDonald, 2015; Abou-El-Enein et al., 2016a,b) as well as an Innovative Medicines Initiative consultation (IMI, 2016) this year have highlighted the major gaps in ATMP development, with manufacturing, regulatory, and reimbursement issues at the forefront, there remains to be formulated a coherent strategy to address these by bringing the relevant stakeholders to a single forum, whose task it would be to design and execute a delta plan to alleviate the most pressing bottlenecks. This article focuses on two of the most urgent areas in need of attention in ATMP development, namely manufacturing and reimbursement, and promotes the concept of innovation-dedicated research infrastructures to support a multi-sector approach for ensuring the successful development, entry, and ensuing survival of ATMPs in the healthcare market.
The mode of inhibition of UDP, one of the products of the reaction catalyzed by (1-.3)-j#-D-glucan synthase in sugar beet (Beta vulgaris L.) was investigated. In the absence of added UDP, the enzyme, in the presence of Ca2", Mg2e, and celiobiose, exhibited Michaelis-Menten kinetics and had an apparent K, of 260 micromolar for UDP-glucose.Complex effects on the kinetics of the (1-.3)-(-D-glucan synthase were observed in the presence of UDP. At high UDP-glucose concentrations, i.e. greater than the apparent K,., UDP behaved as a competitive inhibitor with an apparent K, of 80 micromolar. However, at low UDP-glucose concentrations, reciprocal plots of enzyme activity versus substrate concentration deviated sharply from linearity. This unusual effect of UDP is similar to that reported for fungal (1-.3)-#-D-glucan synthase. However, papulacandin B, a potent inhibitor of this fungal enzyme, had no effect on the plant (1-.3)-ft-D-glucan synthase isolated from sugar beet petioles.The inhibitory effect of UDP was also compared with other known inhibitors of glucan synthases.
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