Molecular structure and subcellular localization of spinach leaf glycolate oxidase

1983 ◽  
Vol 4 (1) ◽  
pp. 99-109 ◽  
Author(s):  
Mikio Nishimura ◽  
Yusuf D. Akhmedov ◽  
Takashi Akazawa
Keyword(s):  
Molecular Structure ◽  
Subcellular Localization ◽  
Glycolate Oxidase ◽  
Spinach Leaf

Molecular structure and subcellular localization of spinach leaf glycolate oxidase

1983 ◽  
Vol 4 (2) ◽  
pp. 99-109 ◽  
Author(s):  
Mikio Nishimura ◽  
Yusuf D. Akhmedov ◽  
Takashi Akazawa
Keyword(s):  
Molecular Structure ◽  
Subcellular Localization ◽  
Glycolate Oxidase ◽  
Spinach Leaf

Pentamethinium fluorescent probes: The impact of molecular structure on photophysical properties and subcellular localization

2014 ◽  
Vol 107 ◽  
pp. 51-59 ◽  
Author(s):  
T. Bříza ◽  
S. Rimpelová ◽  
J. Králová ◽  
K. Záruba ◽  
Z. Kejík ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Subcellular Localization ◽  
Fluorescent Probes ◽  
Photophysical Properties ◽  
The Impact

scholarly journals A Simple Method for Estimating Intactness of Spinach Leaf Protoplasts by Glycolate Oxidase Assay

1985 ◽  
Vol 78 (2) ◽  
pp. 343-346 ◽  
Author(s):  
Mikio Nishimura ◽  
Roland Douce ◽  
Takashi Akazawa
Keyword(s):  
Glycolate Oxidase ◽  
Simple Method ◽  
Spinach Leaf ◽  
Leaf Protoplasts

scholarly journals LOCALIZATION OF ENZYMES WITHIN MICROBODIES

1973 ◽  
Vol 58 (2) ◽  
pp. 379-389 ◽  
Author(s):  
A. H. C. Huang ◽  
H. Beevers
Keyword(s):  
Electron Microscopy ◽  
Rat Liver ◽  
Catalase Activity ◽  
Sucrose Gradient ◽  
Gradient Centrifugation ◽  
Previous Treatment ◽  
Fatty Acyl ◽  
Glycolate Oxidase ◽  
Sucrose Gradient Centrifugation ◽  
Spinach Leaf

Microbodies from rat liver and a variety of plant tissues were osmotically shocked and subsequently centrifuged at 40,000 g for 30 min to yield supernatant and pellet fractions. From rat liver microbodies, all of the uricase activity but little glycolate oxidase or catalase activity were recovered in the pellet, which probably contained the crystalline cores as many other reports had shown. All the measured enzymes in spinach leaf microbodies were solubilized. With microbodies from potato tuber, further sucrose gradient centrifugation of the pellet yielded a fraction at density 1.28 g/cm3 which, presumably representing the crystalline cores, contained 7% of the total catalase activity but no uricase or glycolate oxidase activity. Using microbodies from castor bean endosperm (glyoxysomes), 50–60% of the malate dehydrogenase, fatty acyl CoA dehydrogenase, and crotonase and 90% of the malate synthetase and citrate synthetase were recovered in the pellet, which also contained 96% of the radioactivity when lecithin in the glyoxysomal membrane had been labeled by previous treatment of the tissue with [14C]choline. When the labeled pellet was centrifuged to equilibrium on a sucrose gradient, all the radioactivity, protein, and enzyme activities were recovered together at peak density 1.21–1.22 g/cm3, whereas the original glyoxysomes appeared at density 1.24 g/cm3. Electron microscopy showed that the fraction at 1.21–1.22 g/cm3 was comprised of intact glyoxysomal membranes. All of the membrane-bound enzymes were stripped off with 0.15 M KCl, leaving the "ghosts" still intact as revealed by electron microscopy and sucrose gradient centrifugation. It is concluded that the crystalline cores of plant microbodies contain no uricase and are not particularly enriched with catalase. Some of the enzymes in glyoxysomes are associated with the membranes and this probably has functional significance.

Molecular Structure of the Outermost Cell Wall Component of Spirillum Serpens

1977 ◽  
Vol 35 ◽  
pp. 342-343
Author(s):  
Wah Chiu ◽  
David Grano
Keyword(s):  
Molecular Structure ◽  
Cell Wall ◽  
Outer Membrane ◽  
Gel Electrophoresis ◽  
Electron Microscopic Examination ◽  
Electron Microscopic ◽  
Cell Wall Component ◽  
Protein Components ◽  
Exposure Technique ◽  
Structural Aspects

The periodic structure external to the outer membrane of Spirillum serpens VHA has been isolated by similar procedures to those used by Buckmire and Murray (1). From SDS gel electrophoresis, we have found that the isolated fragments contain several protein components, and that the crystalline structure is composed of a glycoprotein component with a molecular weight of ∽ 140,000 daltons (2). Under an electron microscopic examination, we have visualized the hexagonally-packed glycoprotein subunits, as well as the bilayer profile of the outer membrane. In this paper, we will discuss some structural aspects of the crystalline glycoproteins, based on computer-reconstructed images of the external cell wall fragments.The specimens were prepared for electron microscopy in two ways: negatively stained with 1% PTA, and maintained in a frozen-hydrated state (3). The micrographs were taken with a JEM-100B electron microscope with a field emission gun. The minimum exposure technique was essential for imaging the frozen- hydrated specimens.

Investigating the functional link between TMEM165 and SPCA1

2019 ◽  
Vol 476 (21) ◽  
pp. 3281-3293 ◽  
Author(s):  
Elodie Lebredonchel ◽  
Marine Houdou ◽  
Hans-Heinrich Hoffmann ◽  
Kateryna Kondratska ◽  
Marie-Ange Krzewinski ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Complete Loss ◽  
Protein Family ◽  
Uncharacterized Protein ◽  
Functional Link ◽  
P Type

TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has shown that TMEM165 rapidly degrades with supraphysiological manganese supplementation. In this paper, we establish a functional link between TMEM165 and SPCA1, the Golgi Ca2+/Mn2+ P-type ATPase pump. A nearly complete loss of TMEM165 was observed in SPCA1-deficient Hap1 cells. We demonstrate that TMEM165 was constitutively degraded in lysosomes in the absence of SPCA1. Complementation studies showed that TMEM165 abundance was directly dependent on SPCA1's function and more specifically its capacity to pump Mn2+ from the cytosol into the Golgi lumen. Among SPCA1 mutants that differentially impair Mn2+ and Ca2+ transport, only the Q747A mutant that favors Mn2+ pumping rescues the abundance and Golgi subcellular localization of TMEM165. Interestingly, the overexpression of SERCA2b also rescues the expression of TMEM165. Finally, this paper highlights that TMEM165 expression is linked to the function of SPCA1.

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