scholarly journals Molecular genetic and biochemical characterization of a putative family of zinc metalloproteins in Caenorhabditis elegans

Metallomics ◽  
2018 ◽  
Vol 10 (12) ◽  
pp. 1814-1823 ◽  
Author(s):  
Poulami Chaudhuri ◽  
Hasan Tanvir Imam ◽  
Yona Essig ◽  
Jovaras Krasauskas ◽  
Samuel M. Webb ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Fluorescence Microscopy ◽  
Phase Contrast ◽  
Biochemical Characterization ◽  
Molecular Genetic ◽  
Phase Contrast Microscopy ◽  
C Elegans ◽  
Contrast Microscopy

The first characterization of W08E12.2, W08E12.3, W08E12.4 and W08E12.5, four putative metalloproteins in C. elegans. (A) phase contrast microscopy, (B) fluorescence microscopy of PW08E12.3;W08E12.4::GFP.

Observations by anoptral contrast microscopy of casein in milk, condensed milk and milk powder

1959 ◽  
Vol 26 (2) ◽  
pp. 140-143 ◽  
Author(s):  
N. King
Keyword(s):  
Fluorescence Microscopy ◽  
Phase Contrast ◽  
Milk Powder ◽  
Phase Contrast Microscopy ◽  
Condensed Milk ◽  
Contrast Microscopy ◽  
Thin Membranes

Anoptral contrast, a modification of phase-contrast microscopy, appears to be suitable, particularly perhaps when used in conjunction with fluorescence microscopy, for studying casein particles above 0·1–0·2μ in diameter, and different aggregation and coagulation forms of casein, which may comprise irregular flocks of aggregated particles, thin membranes and micro-fibres, nodulated or smooth.

Identification and molecular-genetic characterization of a LAMP/CD68-like protein from Caenorhabditis elegans

2000 ◽  
Vol 113 (14) ◽  
pp. 2595-2606 ◽  
Author(s):  
M. Kostich ◽  
A. Fire ◽  
D.M. Fambrough
Keyword(s):  
Caenorhabditis Elegans ◽  
Molecular Genetic ◽  
Structural Similarity ◽  
Early Embryo ◽  
C Elegans ◽  
C Terminus ◽  
Apparent Loss ◽  
Membrane Bound ◽  
Molecular Genetic Characterization

Lysosome associated membrane proteins (LAMPs) constitute a family of vertebrate proteins located predominantly in lysosomes, with lesser amounts present in endosomes and at the cell surface. Macrosialin/CD68s are similar to LAMPs in their subcellular distribution and amino acid sequence and presumed structure across the carboxyl terminal two thirds of their length. The functions of LAMPs and CD68s are not known. In the present study, a bioinformatics approach was used to identify a Caenorhabditis elegans protein (LMP-1) with sequence and presumed structural similarity to LAMPs and CD68s. LMP-1 appears to be the only membrane protein in C. elegans that carries a GYXX(phi) vertebrate lysosomal targeting sequence at its C terminus (where (phi) is a large, hydrophobic residue). LMP-1 was found to be present from early embryonic stages through adulthood and to be predominantly localized at the periphery of a population of large, membrane-bound organelles, called granules, that are seen throughout the early embryo but in later stages are restricted to the cells of the intestine. Analysis of an LMP-1 deficient C. elegans mutant revealed that LMP-1 is not required for viability under laboratory conditions, but the absence of LMP-1 leads to an alteration in intestinal granule populations, with apparent loss of one type of granule.

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