scholarly journals In vivo and in vitro synthesis of CM-proteins (A-hordeins) from barley (Hordeum vulgare L.)

Planta ◽  
1983 ◽  
Vol 157 (1) ◽  
pp. 74-80 ◽  
Author(s):  
Javier Paz-Ares ◽  
Fernando Ponz ◽  
Cipriano Aragoncillo ◽  
Carlos Hern�ndez-Lucas ◽  
Gabriel Salcedo ◽  
...  
2010 ◽  
Vol 118 (1) ◽  
pp. 84-89 ◽  
Author(s):  
Yang Qingming ◽  
Pan Xianhui ◽  
Kong Weibao ◽  
Yang Hong ◽  
Su Yidan ◽  
...  

1996 ◽  
Vol 318 (1) ◽  
pp. 279-286 ◽  
Author(s):  
Charles A BREARLEY ◽  
David E HANKE

Partisphere SAX HPLC analysis of endogenous inositol phosphates in [3H]inositol-labelled barley aleurone tissue revealed a range of isomers, including d- and/or l-Ins3P, d- and/or l-Ins(1,4)P2, d- and/or l-Ins(1,2)P2, a third unidentified InsP2, Ins(1,2,3)P3, d- and/or l-Ins(1,2,6)P3, d-and/or l-Ins(1,2,3,4)P4, d- and/or l-Ins(1,2,5,6)P4, Ins(1,3,4,5,6)P5, d- and/or l-Ins(1,2,3,4,5)P5, Ins(1,2,3,4,6)P5, InsP6 and a molecule with the chromatographic properties of an inositol pyrophosphate. The striking match between the identities of the stereoisomers, and in some cases enantiomers, detected in vivo and those stereoisomers produced in vitro by the action of wheat-bran phytase on InsP6 [Cosgrove (1980) Inositol Phosphates: Their Chemistry, Biochemistry and Physiology, Elsevier, Amsterdam] strongly suggests that most of the inositol phosphates identified are products of the breakdown of InsP6 by endogenous phytase(s) with stereospecificity similar to that of the wheat-bran enzyme(s).


Euphytica ◽  
1993 ◽  
Vol 67 (1-2) ◽  
pp. 151-154 ◽  
Author(s):  
A. M. R. Baillie ◽  
B. G. Rossnagel ◽  
K. K. Kartha

2021 ◽  
Author(s):  
Rebecca L Pinals ◽  
Nicholas Ouassil ◽  
Jackson Travis Del Bonis-O'Donnell ◽  
Jeffrey W Wang ◽  
Markita P Landry

Engineered nanoparticles are advantageous for numerous biotechnology applications, including biomolecular sensing and delivery. However, testing the compatibility and function of nanotechnologies in biological systems requires a heuristic approach, where unpredictable biofouling often prevents effective implementation. Such biofouling is the result of spontaneous protein adsorption to the nanoparticle surface, forming the "protein corona" and altering the physicochemical properties, and thus intended function, of the nanotechnology. To better apply engineered nanoparticles in biological systems, herein, we develop a random forest classifier (RFC) trained with proteomic mass spectrometry data that identifies which proteins adsorb to nanoparticles. We model proteins that populate the corona of a single-walled carbon nanotube (SWCNT)-based optical nanosensor. We optimize the classifier and characterize the classifier performance against other models. To evaluate the predictive power of our model, we then apply the classifier to rapidly identify and experimentally validate proteins with high binding affinity to SWCNTs. Using protein properties based solely on amino acid sequence, we further determine protein features associated with increased likelihood of SWCNT binding: proteins with high content of solvent-exposed glycine residues and non-secondary structure-associated amino acids. Furthermore, proteins with high leucine residue content and beta-sheet-associated amino acids are less likely to form the SWCNT protein corona. The classifier presented herein provides an important tool to undertake the otherwise intractable problem of predicting protein-nanoparticle interactions, which is needed for more rapid and effective translation of nanobiotechnologies from in vitro synthesis to in vivo use.


1964 ◽  
Vol 22 (1) ◽  
pp. 227-258 ◽  
Author(s):  
Burton Goldberg ◽  
Howard Green

In vitro synthesis of collagen by established mouse fibroblast lines has been examined by electron microscopy. During rapid growth (log phase), when collagen could not be detected in the cultures, the cells lacked a well developed granular ergastoplasm and Golgi system. Upon cessation of growth (stationary phase), collagen accumulated in the cultures and the cells demonstrated highly developed granular and smooth ergastoplasm. Collagen appeared to be synthesized in the rough-surfaced endoplasmic reticulum and to be transported as a soluble protein to the cell surface by vesicular elements of the agranular ergastoplasm. Fusion of the limiting membranes of these vesicles with the cell membrane permitted the discharge of the soluble collagen into the extracellular space, where fibrils of two diameter distributions formed. The secretion of collagen is concluded to be of the merocrine type. Alternative theories of collagen secretion are discussed and the data for established lines compared with the results of other in vitro and in vivo studies of collagen fibrillogenesis.


1990 ◽  
Vol 129 (4) ◽  
pp. 291-302 ◽  
Author(s):  
R. Hunold ◽  
R. Krämer ◽  
R. Kunert ◽  
H. Peterka

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