38 resultados para CONTAINING POLYMERS


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Letter containing a list of accounts for S.D. Woodruff to accept or reject. This letter is slightly water damaged. This does not affect the text. It is signed by Jarvis, Conklin and Co., n.d.

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Letter containing a memorandum of the work done during Nov. 1855 by Messrs. Brown and McDonell. The work done includes track laying and timber in culverts. There is also a section of the road between St. Catharines and the Great Western Railway where earth has been removed, posts set and laid. This is signed by Francis Lalor, Dec. 12, 1855.

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Letter containing specifications for the construction of the Port Robinson and Thorold macadamized road sent to Matthews from S.D. Woodruff (3 pages, handwritten), Aug. 25, 1855.

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Envelope with a laurel wreath containing the initials W.N. on the back side. The envelope has a 2 cent stamp on it, but it is not addressed, n.d.

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Letter containing a listing of the amounts paid for Lyons Creek. These were sent to S.D. Woodruff from Dexter Deverardo, July 10, 1857.

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Chart containing the statement of amount required to complete the canal, March 15, 1848.

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Studies have demonstrated that the oxysterol binding protein (OSBP) acts as a phosphatidylinositol phosphate (PIP)-sterol exchanger at membrane contact sites (MCS) of the endoplasmic reticulum (ER) and Golgi. OSBP is known to pick up phosphatidylinositol-4-phosphate (PI(4)P) from the ER, transfer it to the trans-Golgi in exchange for a cholesterol molecule that is then transferred from the trans-Golgi to the ER. Upon further examination of this pathway by Ridgway et al. (1), it appeared that phosphorylation of OSBP played a role in the localization of OSBP. The dephosphorylation state of OSBP was linked to Golgi localization and the depletion of cholesterol at the ER. To mimic the phosphorylated state of OSBP, the mutant OSBP-S5E was designed by Ridgway et al. (1). The lipid and sterol recognition by wt-OSBP and its phosphomimic mutant OSBP-S5E were investigated using immobilized lipid bilayers and dual polarization interferometry (DPI). DPI is a technique in which the protein binding affinity to immobilized lipid bilayers is measured and the binding behavior is examined through real time. Lipid bilayers containing 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and varying concentrations of PI(4)Ps or sterols (cholesterol or 25-hydroxycholesterol) were immobilized on a silicon nitride chip. It was determined that wt-OSBP binds differently to PI(4)P-containing bilayers compared to OSBP-S5E. The binding behavior suggested that wt-OSBP extracts PI(4)P and the change in the binding behavior, in the case of OSBP-S5E, suggested that the phosphorylation of OSBP may prevent the recognition and/or extraction of PI(4)P. In the presence of sterols, the overall binding behavior of OSBP, regardless of phosphorylation state, was fairly similar. The maximum specific bound mass of OSBP to sterols did not differ as the concentration of sterols increased. However, comparing the maximum specific bound mass of OSBP to cholesterol with oxysterol (25-hydroxycholesterol), OSBP displayed nearly a 2-fold increase in bound mass. With the absence of the wt-OSBP-PI(4)P binding behavior, it can be speculated that the sterols were not extracted. In addition, the binding behavior of OSBP was further tested using a fluorescence based binding assay. Using 22-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)-23,24-bisnor-5-cholen-3β-ol (22-NBD cholesterol), wt-OSBP a one site binding dissociation constant Kd, of 15 ± 1.4 nM was determined. OSBP-S5E did not bind to 22-NBD cholesterol and Kd value was not obtained.

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Booklet containing Jekyl Island Club charter, constitution, by-laws and members’ names (2 copies). The first copy is missing the membership list and the pages are loose. The spine is taped. The 2nd copy is in good condition, 1887.