Structure of Starch Binding Domains of Halophilic Alpha-Amylase at Low pH

2013 ◽  
Vol 20 (7) ◽  
pp. 755-760 ◽  
Author(s):  
Rui Yamaguchi ◽  
Matsujiro Ishibashi ◽  
Hiroko Tokunaga ◽  
Tsutomu Arakawa ◽  
Masao Tokunaga
Keyword(s):  
Low Ph ◽  
1991 ◽  
Vol 43 (9) ◽  
pp. 355-360 ◽  
Author(s):  
Richard L. Antrim ◽  
Barbara A. Solheim ◽  
Leif Solheim ◽  
Anna-L. Auterinen ◽  
Jerry Cunefare ◽  
...  
Keyword(s):  
Low Ph ◽  

2007 ◽  
Vol 73 (12) ◽  
pp. 3833-3837 ◽  
Author(s):  
D. Guill�n ◽  
M. Santiago ◽  
L. Linares ◽  
R. P�rez ◽  
J. Morlon ◽  
...  

ABSTRACT The Lactobacillus amylovorus alpha-amylase starch binding domain (SBD) is a functional domain responsible for binding to insoluble starch. Structurally, this domain is dissimilar from other reported SBDs because it is composed of five identical tandem modules of 91 amino acids each. To understand adsorption phenomena specific to this SBD, the importance of their modular arrangement in relationship to binding ability was investigated. Peptides corresponding to one, two, three, four, or five modules were expressed as His-tagged proteins. Protein binding assays showed an increased capacity of adsorption as a function of the number of modules, suggesting that each unit of the SBD may act in an additive or synergic way to optimize binding to raw starch.


Author(s):  
J. Quatacker ◽  
W. De Potter

Mucopolysaccharides have been demonstrated biochemically in catecholamine-containing subcellular particles in different rat, cat and ox tissues. As catecholamine-containing granules seem to arise from the Golgi apparatus and some also from the axoplasmic reticulum we examined wether carbohydrate macromolecules could be detected in the small and large dense core vesicles and in structures related to them. To this purpose superior cervical ganglia and irises from rabbit and cat and coeliac ganglia and their axons from dog were subjected to the chromaffin reaction to show the distribution of catecholamine-containing granules. Some material was also embedded in glycolmethacrylate (GMA) and stained with phosphotungstic acid (PTA) at low pH for the detection of carbohydrate macromolecules.The chromaffin reaction in the perikarya reveals mainly large dense core vesicles, but in the axon hillock, the axons and the terminals, the small dense core vesicles are more prominent. In the axons the small granules are sometimes seen inside a reticular network (fig. 1).


2002 ◽  
Vol 69 ◽  
pp. 59-72 ◽  
Author(s):  
Kurt Drickamer ◽  
Andrew J. Fadden

Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are present in vertebrates only. At the cell surface, calcium-dependent (C-type) lectins and galectins are found in model invertebrates and vertebrates, but not in yeast; immunoglobulin superfamily (I-type) lectins are only found in vertebrates. The evolutionary appearance of different classes of sugar-binding protein modules parallels a development towards more complex oligosaccharides that provide increased opportunities for specific recognition phenomena. An overall picture of the lectins present in humans can now be proposed. Based on our knowledge of the structures of several of the C-type carbohydrate-recognition domains, it is possible to suggest ligand-binding activity that may be associated with novel C-type lectin-like domains identified in a systematic screen of the human genome. Further analysis of the sequences of proteins containing these domains can be used as a basis for proposing potential biological functions.


2013 ◽  
Vol 51 (08) ◽  
Author(s):  
V Zevallos ◽  
P Olinga ◽  
Y Junker ◽  
PB Tung ◽  
N Volz ◽  
...  

1964 ◽  
Vol 11 (01) ◽  
pp. 085-093
Author(s):  
W. F Blatt ◽  
JL Gray ◽  
H Jensen

SummaryA sensitive tool has been described for measuring fibrinolysis in reconstituted systems using thrombelastography. Activator mixtures with no appreciable proteolytic activity can similarly be tested in this system when the fibrinogen utilized has sufficient plasminogen present. Exposure of human plasminstreptokinase mixtures formed at pH 7.0 to acid conditions produced a striking loss of activator activity which could not be ascribed to low pH lability of the components, nor to plasmin action on the SK at pH 2.0. This is additional evidence for the hypothesis that human plasmin interacts with SK to form a complex capable of converting human and bovine plasminogen to plasmin.


TAPPI Journal ◽  
2009 ◽  
Vol 8 (2) ◽  
pp. 33-38 ◽  
Author(s):  
ANNA JONHED ◽  
LARS JÄRNSTRÖM

The aim of this study was to investigate the properties of hydrophobically modified (HM) quaterna-ry ammonium starch ethers for paper sizing. These starches possess temperature-responsive properties; that is, gelation or phase separation occurs at a certain temperature upon cooling. This insolubility of the HM starches in water at room temperature improved their performance as sizing agents. The contact angles for water on sized liner were substantially larger than on unsized liner. When the application temperature was well above the critical phase-separation temperature, larger contact angles were obtained for liner independently of pH compared with those at the lower application temperature. Cobb60 values for liner decreased upon surface sizing, with a low pH and high application temperature giving lower water penetration. Contact angles on greaseproof paper decreased upon sur-face sizing as compared to unsized greaseproof paper, independently of pH and temperature. Greaseproof paper showed no great difference between unsized substrates and substrates sized with HM starch at different pH. This is probably due to the already hydrophobic nature of greaseproof paper. However, the Cobb60 values increased at low pH and low application temperature. Surfactants were added to investigate how they affect the sized surface. Addition of surfactant reduces the contact angles, in spite of indications of complex formation.


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