Solution structure and activity of mouse lysozyme M

2003 ◽  
Vol 60 (1) ◽  
pp. 176-184 ◽  
Author(s):  
T. Obita ◽  
T. Ueda ◽  
T. Imoto
Keyword(s):  
Solution Structure ◽  
Mouse Lysozyme ◽  
Structure And Activity

Solution Structure and Activity of the Synthetic Four-Disulfide Bond Mediterranean Mussel Defensin (MGD-1)

Biochemistry ◽  
2000 ◽  
Vol 39 (47) ◽  
pp. 14436-14447 ◽  
Author(s):  
Yin-Shan Yang ◽  
Guillaume Mitta ◽  
Alain Chavanieu ◽  
Bernard Calas ◽  
Jean Frédéric Sanchez ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Solution Structure ◽  
Mediterranean Mussel ◽  
Structure And Activity

scholarly journals Role of proline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5

2002 ◽  
Vol 368 (1) ◽  
pp. 171-182 ◽  
Author(s):  
Sang-Ho PARK ◽  
Hyung-Eun KIM ◽  
Chi-Man KIM ◽  
Hee-Jeong YUN ◽  
Eung-Chil CHOI ◽  
...  
Keyword(s):  
Microbial Activity ◽  
Solution Structure ◽  
Helical Structure ◽  
Haemolytic Activity ◽  
Target Cells ◽  
Disulphide Bridge ◽  
Sds Micelles ◽  
C Terminus ◽  
Structure And Activity

Gaegurin 5 (GGN5) is a cationic 24-residue anti-microbial peptide isolated from the skin of a Korean frog, Rana rugosa. It contains a central proline residue and an intra-residue disulphide bridge in its C-terminus, which are common to the anti-microbial peptides found in Ranidae. We determined the solution structure of GGN5 bound to SDS micelles for the first time and investigated the role of proline, cysteine and a disulphide bridge on the structure and activity of GGN5. GGN5 adopts an amphipathic α-helical structure spanning residues 3—20 kinked around Pro-14, which allows the hydrophobic residues to reside in the concave helical region, and a disulphide-bridged loop-like conformation in its C-terminus. By replacement of proline with alanine (PAGGN5), a straight and rigid helix was formed in the central region and was more stable than the kinked helix. Reduction of a disulphide bridge in the C-terminus (GGN5SH) maintained the loosely ordered loop-like conformation, while the replacement of two cysteines with serines (CSGGN5) caused the C-terminal conformation to be completely disordered. The magnitude of anti-microbial activity of the peptides was closely related to their helical stability in the order PAGGN5>GGN5>GGN5SH>CSGGN5, suggesting that the helical stability of the peptides is important for anti-microbial activity. On the other hand, the significant increase of haemolytic activity of PAGGN5 implies that a helical kink of GGN5 could be involved in the selectivity of target cells. The location of GGN5 and PAGGN5, analysed using paramagnetic probes, was mainly at the surface of SDS micelles, although the location of the N-terminal region was slightly different between them.

scholarly journals pH-Dependent Solution Structure and Activity of a Reduced Form of the Host-Defense Peptide Myticin C (Myt C) from the Mussel Mytilus galloprovincialis

Marine Drugs ◽  
2013 ◽  
Vol 11 (7) ◽  
pp. 2328-2346 ◽  
Author(s):  
Alicia Martinez-Lopez ◽  
Jose Encinar ◽  
Regla Medina-Gali ◽  
Pablo Balseiro ◽  
Pablo Garcia-Valtanen ◽  
...  
Keyword(s):  
Host Defense ◽  
Solution Structure ◽  
Mytilus Galloprovincialis ◽  
Reduced Form ◽  
Host Defense Peptide ◽  
Ph Dependent ◽  
Structure And Activity

Correlative transmission and high-resolution scanning electron microscopic studies on pituitary cells

1990 ◽  
Vol 48 (3) ◽  
pp. 20-21
Author(s):  
S. Tai
Keyword(s):  
Cell Types ◽  
Depth Of Field ◽  
Secretory Cells ◽  
Specific Cell ◽  
Pituitary Cells ◽  
Electron Microscopic ◽  
3 Dimensional ◽  
Microscopic Studies ◽  
Structure And Activity ◽  
Intracellular Structure

Extensive cytological and histological research, correlated with physiological experimental analysis, have been done on the anterior pituitaries of many different vertebrates which have provided the knowledge to create the concept that specific cell types synthesize, store and release their specific hormones. These hormones are stored in or associated with granules. Nevertheless, there are still many doubts - that need further studies, specially on the ultrastructure and physiology of these endocrine cells during the process of synthesis, transport and secretion, whereas some new methods may provide the information about the intracellular structure and activity in detail.In the present work, ultrastructural study of the hormone-secretory cells of chicken pituitaries have been done by using TEM as well as HR-SEM, to correlate the informations obtained from 2-dimensional TEM micrography with the 3-dimensional SEM topographic images, which have a continous surface with larger depth of field that - offers the adventage to interpretate some intracellular structures which were not possible to see using TEM.

Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c

2001 ◽  
Vol 268 (6) ◽  
pp. 1620-1630
Author(s):  
Yibing Wu ◽  
Yunhua Wang ◽  
Chengmin Qian ◽  
Jun Lu ◽  
Ercheng Li ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Solution Structure ◽  
Cytochrome B5

Separation of Heparin into Subtractions by DEAE-Cellulose Chromatography

1979 ◽  
Vol 42 (05) ◽  
pp. 1452-1459 ◽  
Author(s):  
Robert H Yue ◽  
Toby Starr ◽  
Menard M Gertler
Keyword(s):  
High Activity ◽  
Uronic Acid ◽  
Deae Cellulose ◽  
Exchange Chromatography ◽  
Net Charge ◽  
Uronic Acid Content ◽  
Successful Separation ◽  
Salt Gradient ◽  
Structure And Activity ◽  
Low Activity

SummaryCommercial porcine heparin can be separated into three distinct subtractions by using DEAE-cellulose chromatography and a stepped salt gradient. Gram quantities of heparin can be fractionated by this technique. All three heparin subtractions can accelerate the inhibition of thrombin by antithrombin III with different efficiency. The specific activities of the high activity heparin, intermediate activity heparin and low activity heparin are 228 units/mg, 142 units/mg and 95 units/mg, respectively. Both the uronic acid content and the quantity of N-SO4 for all three heparin subfractions have been evaluated. The high activity heparin has the lowest uronic acid and N-SO4 content. The successful separation of commercial heparin into three distinct subfractions by means of ion-exchange chromatography suggests that the net charge on these three heparin components will serve as a model system in the elucidation of the structure and activity relationship to the biological function of heparin.

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