scholarly journals Molecular Structure of WlbB, a BacterialN-Acetyltransferase Involved in the Biosynthesis of 2,3-Diacetamido-2,3-dideoxy-d-mannuronic Acid,

Biochemistry ◽  
2010 ◽  
Vol 49 (22) ◽  
pp. 4644-4653 ◽  
Author(s):  
James B. Thoden ◽  
Hazel M. Holden

2021 ◽  
Author(s):  
S. Giridhar Reddy

Alginates are natural polysaccharides available as seaweed products. They possess several properties due to their molecular structure made of bipolymeric α-L-Guluronic acid and β-D-Mannuronic acid polymers. Alginates have several properties such as film-forming ability, pH responsiveness, and gelling, hydrophilicity, biocompatibility, biodegradability, non-toxic, processability and ionic crosslinking. They’re commonly used in several industries, including food, pharmaceuticals, dental applications, welding rods and scaffolding. Due to their gelling and non-toxic properties, as well as their abundance in nature, the cosmetics and healthcare industries have shown a great deal of interest in biodegradable polymers in general and alginates particularly over the last few decades.



Author(s):  
Wah Chiu ◽  
David Grano

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.





1963 ◽  
Vol 60 ◽  
pp. 52-55
Author(s):  
István Kiss ◽  
Lajos Matus ◽  
István Opauszky


Planta Medica ◽  
2014 ◽  
Vol 80 (10) ◽  
Author(s):  
S Groscurth ◽  
T Kühn ◽  
P Kessler ◽  
V Rukachaisirikul


1966 ◽  
Vol 16 (01/02) ◽  
pp. 018-031 ◽  
Author(s):  
S Sherry ◽  
Norma Alkjaersig ◽  
A. P Fletcher

SummaryComparative studies have been made of the esterase activity of plasmin and the streptokinase-activator of plasminogen on a variety of substituted arginine and lysine esters. Human plasmin preparations derived by different methods of activation (spontaneous in glycerol, trypsin, streptokinase (SK) and urokinase) are similar in their esterase activity; this suggests that the molecular structure required for such esterase activity is similar for all of these human plasmins. Bovine plasmin, on the other hand, differs from human plasmin in its activity on several of the substrates studied (e.g., the methyl esters of benzoyl arginine and tosyl, acetyl and carbobenzoxy lysine), a finding which supports the view that molecular differences exist between the two animal plasmins. The streptokinase-activator hydrolyzes both arginine and lysine esters but the ratios of hydrolytic activity are distinct from those of plasmin and of other activators of plasminogen. The use of benzoyl arginine methyl ester as a substrate for the measurement of the esterase activity of the streptokinase-activator is described.





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