scholarly journals Pathogenesis-Related PR-1 Proteins Are Antifungal (Isolation and Characterization of Three 14-Kilodalton Proteins of Tomato and of a Basic PR-1 of Tobacco with Inhibitory Activity against Phytophthora infestans)

1995 ◽  
Vol 108 (1) ◽  
pp. 17-27 ◽  
Author(s):  
T. Niderman ◽  
I. Genetet ◽  
T. Bruyere ◽  
R. Gees ◽  
A. Stintzi ◽  
...  
2013 ◽  
Vol 85 ◽  
pp. 129-136 ◽  
Author(s):  
Lin-Wen Lee ◽  
Guei-Jane Wang ◽  
Mei-Hsiang Lin ◽  
Yu-Min Ju ◽  
Yen-Wen Lin ◽  
...  

1990 ◽  
Vol 14 (3) ◽  
pp. 381-390 ◽  
Author(s):  
Serge Kauffmann ◽  
Michel Legrand ◽  
Bernard Fritig

2015 ◽  
Vol 2 (1) ◽  
pp. 114 ◽  
Author(s):  
Enjuro Harunari ◽  
Chiaki Imada ◽  
Yasuhiro Igarashi ◽  
Takao Fukuda ◽  
Takeshi Terahara ◽  
...  

A novel hyaluronidase inhibitor (HI) was isolated from the culture extract of a marine- derived actinomycete strain. This strain MB-PO13 was isolated from ascidian (Molgula manhattensis) in Tokyo Bay. Out of about 1,000 isolates from various marine organisms, strain MB-PO13 had the strongest inhibitory activity and was selected for further study. The strain showed abundant-to-moderate growth on most media, forming a grayish mycelium. On the basis of the taxonomical characteristics, the strain was classified as belonging to the genus of Streptomyces and was named as Streptomyces sp. strain MB-PO13. The structure of HI was elucidated by interpretation of NMR data. HI displayed about 25-fold potent hyaluronidase inhibitory activity against hyaluronidase than glycyrrhizin. Keywords: marine actinomycetes; Streptomyces; hyaluronidase inhibitor 


1983 ◽  
Vol 209 (1) ◽  
pp. 91-97 ◽  
Author(s):  
R T Jacob ◽  
P G Bhat ◽  
T N Pattabiraman

A specific enterokinase inhibitor from kidney bean (Phaseolus vulgaris) was purified to homogeneity. It showed a single protein band on sodium dodecyl sulphate/polyacryl-amide-gel electrophoresis in the presence of mercaptoethanol, and the Mr was 31000. Aspartic acid was identified as the N-terminus of the inhibitor. The Mr by gel chromatography on Sephadex G-200 was found to be 60000, indicating the dimeric nature of the inhibitor. The inhibitor was found to be a glycoprotein. The monosaccharide moieties were glucose, mannose, glucuronic acid and glucosamine in the proportions 3.15%, 5.0%, 0.85% and 1.3% respectively. The inhibitor was most active on pig enterokinase, followed by bovine and human enterokinases. Maximal inhibitory activity was elicited by preincubation of the inhibitor with the enzyme for 15 min. Digestion with pepsin resulted in loss of inhibitory activity. The inhibitor was stable to exposure to a wide range of pH values (2-10), and exposure to pH above 10 resulted in loss of inhibitory activity. Modification of arginine residues by cyclohexane 1,2-dione and ninhydrin led to complete loss of enterokinase-inhibitory activity.


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