Active fragments of a filamentous bacteriophage

1966 ◽  
Vol 25 (3) ◽  
pp. 275-284 ◽  
Author(s):  
George Fareed ◽  
Karin A. Ippen ◽  
Raymond C. Valentine
Keyword(s):  
Filamentous Bacteriophage ◽  
Active Fragments

Permeability Enhancing and Chemotactic Activities of Lower Molecular Weight Degradation Products of Human Fibrinogen

1981 ◽  
Vol 45 (01) ◽  
pp. 090-094 ◽  
Author(s):  
Katsuo Sueishi ◽  
Shigeru Nanno ◽  
Kenzo Tanaka
Keyword(s):  
Molecular Weight ◽  
Degradation Products ◽  
Electron Microscopic Observation ◽  
Chemotactic Activity ◽  
Lower Molecular Weight ◽  
Electron Microscopic ◽  
Human Fibrinogen ◽  
Rabbit Skin ◽  
Molecular Weights ◽  
Active Fragments

SummaryFibrinogen degradation products were investigated for leukocyte chemotactic activity and for enhancement of vascular permeability. Both activities increased progressively with plasmin digestion of fibrinogen. Active fragments were partially purified from 24 hr-plasmin digests. Molecular weights of the permeability increasing and chemotactic activity fractions were 25,000-15,000 and 25,000 respectively. Both fractions had much higher activities than the fragment X, Y, D or E. Electron microscopic observation of the small blood vessels in rabbit skin correlated increased permeability with the formation of characteristic gaps between adjoining endothelial cells and their contraction.These findings suggest that lower molecular weight degradation products of fibrinogen may be influential in contributing to granulocytic infiltration and enhanced permeability in lesions characterized by deposits of fibrin and/or fibrinogen.

pH-Degradable imidazolium oligomers as antimicrobial materials with tuneable loss of activity

2019 ◽  
Vol 7 (6) ◽  
pp. 2317-2325 ◽  
Author(s):  
Yuan Yuan ◽  
Diane S. W. Lim ◽  
Hong Wu ◽  
Hongfang Lu ◽  
Yiran Zheng ◽  
...  
Keyword(s):  
Bacterial Resistance ◽  
Ph Sensitive ◽  
Antimicrobial Materials ◽  
Active Fragments

Imidazolium oligomers containing pH-sensitive linkers degrade under basic conditions to less active fragments that slow the development of bacterial resistance.

scholarly journals Active fragments obtained by cyanogen bromide cleavage of ovomucoid

1976 ◽  
Vol 155 (2) ◽  
pp. 345-351 ◽  
Author(s):  
J G. Beeley
Keyword(s):  
Molecular Weight ◽  
Trypsin Inhibitor ◽  
Inhibitory Activity ◽  
Cyanogen Bromide ◽  
Peptide Chain ◽  
Terminal Portion ◽  
Trypsin Inhibitory Activity ◽  
Methionine Residues ◽  
Active Fragments

Cleavage of the two methionine residues in the glycoprotein trypsin inhibitor ovomucoid, variant O1, with CNBr resulted in two fragments whose mol.wts. were approx. 16 600 (fragment LS) and 11 000 (fragment M). Both fragments formed precipitates with antisera to ovomucoid. Fragment LS retained 56% of the trypsin-inhibitory activity of ovomucoid, but fragment M did not inhibit. After reduction and alkylation, the molecular weight of fragment M was unchanged, but fragment LS could be resolved into two segments of peptide chain with mol.wts. of approx. 12000 (fragment L) and 4700 (fragment S). Each of these peptides contained carbohydrate. Marked heterogeneity was observed in the hexose and hexosamine contents of fragment L. This may account for much of the heterogeneity in neutral carbohydrate occurring in ovomucoid preparations. It was found that fragment M was located at the N-terminal end, fragment S was in the centre and fragment L made up the C-terminal portion of the molecule.

scholarly journals A strategy of exon shuffling for making large peptide repertoires displayed on filamentous bacteriophage.

1996 ◽  
Vol 93 (15) ◽  
pp. 7761-7766 ◽  
Author(s):  
I. Fisch ◽  
R. E. Kontermann ◽  
R. Finnern ◽  
O. Hartley ◽  
A. S. Soler-Gonzalez ◽  
...  
Keyword(s):  
Exon Shuffling ◽  
Filamentous Bacteriophage ◽  
Large Peptide
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