Results 21 to 30 of about 63,707 (195)

Engineering Saccharomyces cerevisiae for the production and secretion of Affibody molecules

Microbial Cell Factories, 2022
Background Affibody molecules are synthetic peptides with a variety of therapeutic and diagnostic applications. To date, Affibody molecules have mainly been produced by the bacterial production host Escherichia coli.
Veronica Gast, Anna Sandegren, Finn Dunås, Siri Ekblad, Rezan Güler, Staffan Thorén, Marta Tous Mohedano, Mikael Molin, Martin K. M. Engqvist, Verena Siewers   +9 more
doaj   +1 more source

Porcine Carboxypeptidase B [PDF]

European Journal of Biochemistry, 1972
Porcine carboxypeptidase B is inhibited rapidly by nitration with an eight‐fold molar excess of tetranitromethane. Enzymie activity towards both basic and non‐basic substrates falls to less than 30% of the control. The loss of activity correlates with the nitration of a single tyrosyl residue.
M, Sokolovsky, L, Eisenbach
openaire   +5 more sources

Altered proteome of a Burkholderia pseudomallei mutant defective in short-chain dehydrogenase affects cell adhesion, biofilm formation and heat stress tolerance [PDF]

PeerJ, 2020
Burkholderia pseudomallei is a Gram-negative bacillus that causes melioidosis and is recognized as an important public health problem in southeast Asia and northeast Australia. The treatment of B.
Onrapak Reamtong, Nitaya Indrawattana, Amporn Rungruengkitkun, Tipparat Thiangtrongjit, Taksaon Duangurai, Manas Chongsa-nguan, Pornpan Pumirat   +6 more
doaj   +2 more sources

Anabaenopeptin B Chlorination Degradation By-Products Retain Potent Carboxypeptidase B Inhibition. [PDF]

ACS ES T Water
Stringer BB, Quandt ML, Thenuwara SI, Peraino NJ, Kodanko JJ, Westrick JA.   +5 more
europepmc   +2 more sources

The variation of two extracellular enzymes and soybean meal bitterness during solid-state fermentation of Bacillus subtilis

Grain & Oil Science and Technology, 2019
The debittering effect of extracellular enzymes from Bacillus subtilis ACCC 01746 was studied using soybean meal as a substrate for solid-state fermentation (SSF). Results showed that B. subtilis produces proteases and carboxypeptidase in the early stage
Haicheng Yin, Feng Jia, Jin Huang
doaj   +1 more source

Peptide Inhibitors and Activators of Carboxypeptidase B [PDF]

European Journal of Biochemistry, 1973
A number of peptides containing d‐residues at the penultimate or C‐terminal position were tested for their ability to affect the carboxypeptidase‐B‐catalysed hydrolysis of basic and non‐basic peptides and esters. The effect of these modifiers, i.e. activation or inhibition is dependent on the nature of the modifier.
N, Zisapel, N, Kurn-Abramowitz, M, Sokolovsky   +2 more
openaire   +2 more sources

[20] Carboxypeptidases A and B [PDF]

Proceedings of the National Academy of Sciences, 1977
Publisher Summary Carboxypeptidases A (EC 3.4.12.2) and B (EC 3.4.12.3) are pancreatic exopeptidases. carboxypeptidase A preferentially hydrolyzes terminal peptide bonds in which the amino donor is a hydrophobic amino acid whereas the specificity of carboxypeptidase B is directed toward the terminal basic amino acids.
K, Titani, L H, Ericsson, K A, Walsh, H, Neurath   +3 more
openaire   +3 more sources

Design of Primers for Detection and Typing of β-Lactamase Genes from Pathogenic Species of Burkholderia

Проблемы особо опасных инфекций, 2012
The set of oligonucleotide primers was designed to identify β-lactam-resitance determinats in isolates of pathogenic Burkholderia using PCR. Simultaneously identified was certain molecular class of detected β-lactamases.
A. V. Romanova, I. B. Zakharova, V. S. Zamaraev, D. V. Viktorov   +3 more
doaj   +1 more source

A Seed-Endophytic Bacillus safensis Strain With Antimicrobial Activity Has Genes for Novel Bacteriocin-Like Antimicrobial Peptides

Frontiers in Microbiology, 2021
Bacteriocins are a highly diverse group of antimicrobial peptides that have been identified in a wide range of commensal and probiotic organisms, especially those resident in host microbiomes.
Jeanne Romero-Severson, Thomas E. Moran, Donna G. Shrader, Francisco R. Fields, Susan Pandey-Joshi, Clayton L. Thomas, Emily C. Palmer, Emily C. Palmer, Joshua D. Shrout, Joshua D. Shrout, Michael E. Pfrender, Shaun W. Lee   +11 more
doaj   +1 more source

Purification of carboxypeptidase B from human pancreas [PDF]

Biochemical Journal, 1977
Carboxypeptidase B of the human pancreas was purified by chromatography on DEAE-cellulose and CM-cellulose columns. Two forms of the enzyme, named carboxypeptidase B1 and B2, were separated. They have similar mol.wts. (34250 +/- 590) as established by polyacrylamide-gel disc electrophoresis and by gel filtration.
D V, Marinkovic, J N, Marinkovic, E G, Erdös, C J, Robinson   +3 more
openaire   +2 more sources