Biosynthesis of glycosylated human lysozyme mutants
نویسندگان
چکیده
منابع مشابه
Biosynthesis of glycosylated human lysozyme mutants.
Complementary DNA encoding human lysozyme was subjected to oligonucleotide-directed mutagenesis. At one of three selected positions, amino acid residues 22, 68, or 118, the signal for N-linked glycosylation was created. The mutant DNAs were inserted into a eucaryotic vector and transfected into cultured hamster cells. The three mutant cDNAs directed synthesis of lysozyme mutants, which were nam...
متن کاملIsolation and characterization of lysozyme-sensitive mutants of Staphylococcus aureus.
Four lysozyme-sensitive mutants were isolated after nitrosoguanidine mutagenesis of a lysozyme-insensitive strain of Staphylococcus aureus. One mutant was sufficiently effective for the isolation of macromolecules, such as plasmid deoxyribonucleic acids, from a cell after lysozyme-induced cell lysis.
متن کاملDraft Genome Sequences of Salmonella Lysozyme Gene Knockout Mutants
Lysozyme enzymes hydrolyze the β-1,4-glycosidic bond in oligosaccharides. These enzymes are part of a broad group of glucoside hydrolases that are poorly characterized; however, they are important for growth and are being recognized as emerging virulence factors. This is the release of four lysozyme-encoding-gene-deletion mutants in Salmonella enterica serovar Typhimurium LT2.
متن کاملIsolation of mutants blocked in calicheamicin biosynthesis.
Blocked mutants of Micromonospora echinospora defective in the production of the potent antitumor agent calicheamicin are described. Analysis of intermediates produced by blocked mutants indicates a branched biosynthetic pathway. Mutants that produced some, but not all, calicheamicin forms are also described.
متن کاملHuman cartilage lysozyme.
The lysozyme content of human cartilage was measured by incubation of lyophilized, powdered cartilage in a variety of buffers and salt solutions, and the factors controlling the binding of lysozyme within cartilage were studied. Lysozyme was extracted from hyaline cartilage by buffers of pH greater than 9.0 by solutions 1 M in monovalent cations, and by solutions 0.12-0.40 M in divalent cations...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)92788-2