x-Ray Diffraction Studies of Built-up Films of Long-Chain Compounds

1935 ◽  
Vol 57 (2) ◽  
pp. 330-331 ◽  
Author(s):  
G. L. Clark ◽  
R. R. Sterrett ◽  
P. W. Leppla
Keyword(s):  
X Ray Diffraction ◽  
X Ray ◽  
Chain Compounds ◽  
Long Chain

The Epicuticle of an Arachnid, Palamneus swammerdami

1954 ◽  
Vol s3-95 (31) ◽  
pp. 371-381
Author(s):  
G. KRISHNAN
Keyword(s):  
Outer Membrane ◽  
Diffraction Pattern ◽  
Basal Layer ◽  
Thin Membrane ◽  
Basic Pattern ◽  
X Ray Diffraction ◽  
X Ray ◽  
Chemical Constitution ◽  
Long Chain

The epicuticle of Palamneus swammerdami in the unhardened condition is homogeneous. It stains uniformly red with Mallory. When hardened, it comprises an internal unstained region, giving evidence of --S--S-- bonding, and is bounded externally by a very thin membrane which stains blue with Mallory. The protein of the inner basal layer differs from its counterpart in the insect epicuticle in the absence of tyrosine, in the occurrence of cystine and cysteine, and in being resistant to the action of hot alkalis. Though apparently related to the keratin of vertebrates, it is not identical with it. The outer thin membrane is lipide in nature. X-ray diffraction studies show that the epicuticular protein is unique: it is unlike both arthropodin and the keratin of vertebrates. However, the outer membrane of the epicuticle yields a diffraction pattern indicating the presence of long-chain paraffins and is similar to the outer epicuticle of the blowfly larva. The chitin of the cuticle appears to be identical in pattern with that of insects. In spite of differences in structural and chemical constitution, the epicuticle of the scorpion shows a resemblance to the basic pattern of the insect epicuticle. The differences may be attributed to the absence of phenolic tanning and the occurrence of --S--S-- bonding. The possible role of the purines present in the cuticle of the scorpion is discussed in relation to --S--S-- bonding.

Anti-mycobacterial activities of copper(II) salicylaldimine complexes derived from long-chain aliphatic amines

2013 ◽  
Vol 91 (11) ◽  
pp. 1093-1097 ◽  
Author(s):  
Alyssa E. Patterson ◽  
Eric G. Bowes ◽  
Allyson Bos ◽  
Taryn O’Neill ◽  
Haoxin Li ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Schiff Base ◽  
Aliphatic Amines ◽  
Schiff Base Complexes ◽  
Aliphatic Chain ◽  
X Ray Diffraction ◽  
X Ray ◽  
Microwave Assisted ◽  
Long Chain

Twelve copper(II) Schiff base complexes derived from lipophilic amines have been prepared using either salicylaldehyde or ortho-vanillin via a microwave-assisted reaction. All complexes have been obtained elementally pure and an X-ray diffraction of an isopentyl derivative has confirmed the structure of these compounds. All complexes showed a promising degree of anti-mycobacterial activity against Mycobacterium tuberculosis, where activity seemed to increase with an increase in the length of the aliphatic chain.

The Influence of Emulsifiers on the Crystal Properties of Tristearin and Trilaurin

1988 ◽  
Vol 3 (1) ◽  
pp. 19-22 ◽  
Author(s):  
J. Schlichter ◽  
I. Mayer ◽  
S. Sarig ◽  
N. Garti
Keyword(s):  
Crystal Structure ◽  
Melting Point ◽  
Diffraction Method ◽  
The Other ◽  
Sorbitan Monostearate ◽  
X Ray Diffraction ◽  
Sorbitan Monolaurate ◽  
X Ray ◽  
Crystal Properties ◽  
Long Chain

AbstractThe effect of solid emulsifiers, added at the level of 10%, on the lattice parameters of tristearin and trilaurin, has been studied by powder X-ray diffraction method. The presence of sorbitan monostearate and glycerol-l-stearate affects slightly the lattice constant a in tristearin; on the other hand, although sorbitan monostearate causes an increase in a of trilaurin, glycerol-l-stearate does not. The presence of sorbitan monolaurate and glycerol-l-laurate affect a of trilaurin similarly to the long chain emulsifiers.A correlation between the effect on a and the increase in melting point has been found.The presence of the emulsifier does not alter drastically the lattice dimensions of the fat. The slight dissimilarity in crystal structure between tristearin and trilaurin is confirmed by the diverse effects of the emulsifiers on the internal structure of the fat.

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