Foam-like GaN: Study on the controlled tuning of pore size by R group change in amino acid etchant and its ultra-high photocurrent response

Vacuum ◽  
2021 ◽  
pp. 110779
Author(s):  
Zi'ang Zhang ◽  
Long Zhang ◽  
Zeng Liu ◽  
Kaikai Li ◽  
Lifan Nie ◽  
...  
2019 ◽  
Vol 45 (13) ◽  
pp. 1051-1057 ◽  
Author(s):  
Liangning Gu ◽  
Qibin Chen ◽  
Xiaoxiao Li ◽  
Chenchen Meng ◽  
Honglai Liu

Author(s):  
Xiaoxiao Li ◽  
Chenchen Meng ◽  
Yan Meng ◽  
Liangning Gu ◽  
Qibin Chen ◽  
...  

1987 ◽  
Vol 115 (1) ◽  
pp. 47-51
Author(s):  
F. A. Duffy ◽  
A. M. Wallace

ABSTRACT The size of molecules able to be measured in immunoassays where antibody is encapsulated within semipermeable microcapsules is restricted by the pore size of the membrane. This study was performed to determine the approximate molecular weight cut-off of this membrane. Permeability was assessed by measuring which labelled hormones were able to enter and bind their respective microencapsulated antibody. Hormones with molecular weights of less than 4000 (angiotensin II, thyroxine, 17-hydroxyprogesterone, progesterone, testosterone and androstenedione) passed freely through the pores but larger molecules, with molecular weights in excess of 10 000 (parathyroid hormone, human GH, TSH) could not. Insulin, with a molecular weight of 6000 (approximate minimum diameter 3·5 nm), had restricted entry while the next smallest hormone tested, the 1–34 amino acid portion of parathyroid hormone (molecular weight 4000; diameter 1·8 nm), was able to bind encapsulated antibody, suggesting that the pore diameter is between 1·8 and 3·5 nm. It can now be predicted that the method is able to measure compounds with a diameter within this range and with a molecular weight below 6000. Microcapsules may be useful for improving specificity of assays where a cross-reactant is too large to penetrate the membrane. J. Endocr. (1987) 115, 47–51


Author(s):  
Lawrence W. Ortiz ◽  
Bonnie L. Isom

A procedure is described for the quantitative transfer of fibers and particulates collected on membrane filters to electron microscope (EM) grids. Various Millipore MF filters (Millipore AA, HA, GS, and VM; 0.8, 0.45, 0.22 and 0.05 μm mean pore size) have been used with success. Observed particle losses have not been size dependent and have not exceeded 10%. With fibers (glass or asbestos) as the collected media this observed loss is approximately 3%.


Author(s):  
M.K. Lamvik ◽  
L.L. Klatt

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.


Author(s):  
A. J. Tousimis

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.


Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.


Author(s):  
Eduardo A. Kamenetzky ◽  
David A. Ley

The microstructure of polyacrylonitrile (PAN) beads for affinity chromatography bioseparations was studied by TEM of stained ultramicrotomed thin-sections. Microstructural aspects such as overall pore size distribution, the distribution of pores within the beads, and surface coverage of functionalized beads affect performance properties. Stereological methods are used to quantify the internal structure of these chromatographic supports. Details of the process for making the PAN beads are given elsewhere. TEM specimens were obtained by vacuum impregnation with a low-viscosity epoxy and sectioning with a diamond knife. The beads can be observed unstained. However, different surface functionalities can be made evident by selective staining. Amide surface coverage was studied by staining in vapor of a 0.5.% RuO4 aqueous solution for 1 h. RuO4 does not stain PAN but stains, amongst many others, polymers containing an amide moiety.


1979 ◽  
Vol 7 (1) ◽  
pp. 261-262
Author(s):  
E. V. ROWSELL

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