Biochemical studies on pili isolated from Pseudomonas aeruginosa strain PAO

1979 ◽  
Vol 25 (10) ◽  
pp. 1175-1181 ◽  
Author(s):  
W. Paranchych ◽  
P. A. Sastry ◽  
L. S. Frost ◽  
M. Carpenter ◽  
G. D. Armstrong ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Biochemical Characterization ◽  
Average Length ◽  
Amino Terminus ◽  
Amino Acid Residues ◽  
Present Communication ◽  
Amino Terminal ◽  
Single Polypeptide

Pseudomonas aeruginosa strains PAO and PAK bear polar pili which are flexible filaments having a diameter of 6 nm and an average length of 2500 nm. Both types of pili are retractile and promote infection by a number of bacteriophages. The present communication describes the partial biochemical characterization of PAO pili isolated from a multipiliated nonretractile mutant of PAO. The observed properties are compared to those of PAK pili which were characterized previously. PAO pili were found to contain a single polypeptide subunit of 18 700 daltons. This is similar to PAK pili which contain a single polypeptide of 18 100 daltons. The amino acid composition of PAO pilin was also similar to that of PAK pilin. Neither protein contained phosphate or carbohydrate residues and both were found to contain N-methylphenylalanine at the amino terminus. Sequencing of 20 amino acid residues at the amino terminal end of PAO pilin revealed the sequence to be identical with that of PAK pilin, while tryptic peptide analyses of PAO and PAK pilin indicated that the two proteins probably contain a number of homologous regions within the polypeptide. It was concluded that PAO and PAK pili are closely related structures.

CHARACTERIZATION OF TYPES OF STAPHYLOCOCCAL ENTEROTOXI NS1,2

1973 ◽  
Vol 36 (12) ◽  
pp. 610-612 ◽  
Author(s):  
Merlin S. Bergdoll ◽  
Ruth N. Robbins
Keyword(s):  
Amino Acid ◽  
Antigenic Site ◽  
The Other ◽  
Amino Acid Residues ◽  
Staphylococcal Enterotoxins ◽  
Single Polypeptide ◽  
Polypeptide Chains

The staphylococcal enterotoxins are single polypeptide chains that contain two half-cystine residues that are cross-linked in the native toxin to form a “cystine” loop. Several amino acid residues involving part of this loop appear to be the same for the different enterotoxins which may represent the toxic site. The other part of the cystine loop may be involved in the antigenicity of the toxin which is the basis for identifying them as enterotoxns A-E. The antigenicty of the enterotoxins varies from the similarity of enterotoxins C1 and C2 which have the same major antigenic site to enterotoxins A and B which are apparently unrelated antigenically.

scholarly journals The amino acid sequence of ferredoxin from Brassica napus (rape)

1980 ◽  
Vol 185 (1) ◽  
pp. 239-243 ◽  
Author(s):  
I Takruri ◽  
D Boulter
Keyword(s):  
Amino Acid ◽  
Brassica Napus ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Plant Type ◽  
Single Polypeptide Chain ◽  
N Terminus ◽  
Single Polypeptide

The amino acid sequence of the ferredoxin of Brassica napus was determined by using a Beckman 890C sequencer in combination with the characterization of peptides obtained by tryptic and chymotryptic digestion of the protein; some peptides were subdigested with thermolysin. The molecule consists of a single polypeptide chain of 96 amino acid residues and has an unblocked N-terminus. The primary structure shows considerable similarity with other plant-type ferredoxins.

Adult amphibian epidermal proteins: biochemical characterization and developmental appearance

Development ◽  
1975 ◽  
Vol 34 (1) ◽  
pp. 55-73
Author(s):  
O. Raymond Reeves
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Biochemical Characterization ◽  
Peptide Mapping ◽  
Polyacrylamide Gel Electrophoresis ◽  
Group Analysis ◽  
Amphibian Skin ◽  
Antibody Preparation ◽  
Amino Terminal

The keratin-like proteins (KLPs) from the epidermis of adult frogs of the species Xenopus laevis have been isolated and biochemically characterized by means of polyacrylamide gel electrophoresis, amino acid analysis, tryptic peptide mapping, amino-terminal end-group analysis and isoelectric focusing. One particular protein fraction of rather unusual amino acid composition found only in epidermal tissue was isolated in quantity by preparative gel electrophoresis and monospecific antibodies prepared against it. Using this anti-KLP antibody preparation it was possible to show that at least one kind of keratin-like protein characteristic of the adult epidermis first appears within the larval epidermis during metamorphosis. This is the first reported biochemical characterization of a tissue-specific proteinfrom adult amphibian skin.

scholarly journals Biochemical Characterization of a Prokaryotic Phenylalanine Ammonia Lyase

2005 ◽  
Vol 187 (12) ◽  
pp. 4286-4289 ◽  
Author(s):  
Longkuan Xiang ◽  
Bradley S. Moore
Keyword(s):  
Amino Acid ◽  
Cinnamic Acid ◽  
Marine Bacterium ◽  
Phenylalanine Ammonia Lyase ◽  
Biochemical Characterization ◽  
The Novel ◽  
Amino Acid Residues ◽  
Primary Amino ◽  
Biochemical Features

ABSTRACT The committed biosynthetic reaction to benzoyl-coenzyme A in the marine bacterium “Streptomyces maritimus” is carried out by the novel prokaryotic phenylalanine ammonia lyase (PAL) EncP, which converts the primary amino acid l-phenylalanine to trans-cinnamic acid. Recombinant EncP is specific for l-phenylalanine and shares many biochemical features with eukaryotic PALs, which are substantially larger proteins by ∼200 amino acid residues.

Biochemical characterization of HIV-1 reverse transcriptases encoding mutations at amino acid residues 161 and 208 involved in resistance to phosphonoformate

1998 ◽  
Vol 56 (12) ◽  
pp. 1583-1589 ◽  
Author(s):  
Enzo Tramontano ◽  
Giovanna Piras ◽  
John W Mellors ◽  
Monica Putzolu ◽  
Hengameh Z Bazmi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biochemical Characterization ◽  
Amino Acid Residues ◽  
Reverse Transcriptases ◽  
Hiv 1

Properties of a non collagen-degradingBacillus subtiliskeratinase

2008 ◽  
Vol 54 (3) ◽  
pp. 180-188 ◽  
Author(s):  
Alexandre José Macedo ◽  
Walter Orlando Beys da Silva ◽  
Carlos Termignoni
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Molecular Mass ◽  
Biochemical Characterization ◽  
Detectable Effect ◽  
Amino Acid Residues ◽  
Keratinolytic Activity ◽  
Biotechnological Potential ◽  
Optimum Ph

Bacillus subtilis S14 produces a keratinase (KerS14) with non collagen-degrading activity. Indeed, this is the first keratinase described so far that does not have any detectable effect on collagen, which is a crucial property for an enzyme intended to be used in skin dehairing. Because of its importance as an industrial tanning enzyme, we report the biochemical characterization of KerS14. This protein exhibited an apparent molecular mass of 27 kDa, a pI of 6.5, and an optimum pH in the range of 8.0–9.0. The enzyme’s activity was stimulated by Mn2+(7.7-fold), Ca2+(6.1-fold), Mg2+(4.9-fold), and Co2+(4.0-fold) but was inhibited by Cu2+and Zn2+. Using p-nitroanilide and methylcoumarine derivatized peptides, we observed that KerS14 prefered Arg at subsite P1, small amino acid residues at subsite P2, and Gln or Glu at subsite P3. KerS14 presented higher keratin degradation specificity than other commercial proteases. Its high keratinolytic activity and the absence of virtually any activity against collagen remark the biotechnological potential of this enzyme to be used at larger scales in tannery dehairing processes.

scholarly journals Amino Acid Sequence of the a-Chain of the Tetrameric Haemoglobin of the Bivalve Mollusc Anadara Trapezia

1980 ◽  
Vol 33 (6) ◽  
pp. 653 ◽  
Author(s):  
PF Como ◽  
EOP Thompson
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Amino Acid ◽  
Magnetic Resonance ◽  
Amino Acid Sequence ◽  
Bivalve Mollusc ◽  
Amino Terminus ◽  
Spectrographic Analysis ◽  
Amino Acid Residues ◽  
Amino Terminal ◽  
A Chain

The amino acid sequence of the IX-chain of the tetrameric haemoglobin of the bivalve mollusc A. trapezia shows 153 amino acid residues, longer than invertebrate globins previously sequenced. The amino terminal residue is acetylated as shown by nuclear magnetic resonance and mass spectrographic analysis of an N-terminal peptide. There are additional residues at the amino terminus, similar to the IX-globin of the shark and lamprey globin. In common with other invertebrate globin sequences, when compared with vertebrate globins it is necessary to insert extra gaps in interhelical regions of the vertebrate alignment to preserve homology.

Sign in / Sign up

Export Citation Format

Share Document