Zobrazeno 1 - 9
of 9
pro vyhledávání: '"J M, Gleisner"'
Autor:
J M Gleisner, R L Blakley
Publikováno v:
Journal of Biological Chemistry. 250:1580-1587
Carboxymethylation by iodoacetate of dihydrofolate reductase from the amethopterin-resistant mutant Streptococcus faecium var. Durans strain A leads to a loss of enzymic activity. Amino acid analysis showed that methionine is the only amino acid resi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::52aceece88e4510cf44f39b4f71f78ae
https://doi.org/10.1016/s0021-9258(19)41848-6
https://doi.org/10.1016/s0021-9258(19)41848-6
Publikováno v:
Journal of Biological Chemistry. 250:4945-4954
The complete amino acid sequence of the mutant dihydrofolate reductase from Streptococcus faecium var. Durans strain A has been determined by sequence analysis of peptides produced by tryptic, chymotryptic, thermolytic, and mild acid cleavage of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12f5ae2ed8f05843ebbe14000bee5377
https://doi.org/10.1016/s0021-9258(19)41260-x
https://doi.org/10.1016/s0021-9258(19)41260-x
Publikováno v:
Journal of Biological Chemistry. 250:4937-4944
The major form of dihydrofolate reductase from a methotrexate-resistant mutant (strain A) of Streptococcus faecium var. Durans has been purified on a large scale. Amino acid analysis of this form of the enzyme (isoenzyme 2) reveals an absence of cyst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4843ba42a903d31d272e1dd531ae9447
https://doi.org/10.1016/s0021-9258(19)41259-3
https://doi.org/10.1016/s0021-9258(19)41259-3
Publikováno v:
The Journal of biological chemistry. 250(13)
The major form of dihydrofolate reductase from a methotrexate-resistant mutant (strain A) of Streptococcus faecium var. Durans has been purified on a large scale. Amino acid analysis of this form of the enzyme (isoenzyme 2) reveals an absence of cyst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dce4e15a565da7408ef486dd6d8b3ab0
https://pubmed.ncbi.nlm.nih.gov/1150647
https://pubmed.ncbi.nlm.nih.gov/1150647
Autor:
J M, Gleisner, C A, Ramthun
Publikováno v:
Microbios. 32(127)
The aminopeptidase activity of three strains of Mycobacterium tuberculosis, H37Rv, H37Ra, and M. tuberculosis from a patient, was partially purified and characterized. The activity from all three organisms was found to be very similar, if not identic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::60220fd28307b63870e583bd9c817568
https://pubmed.ncbi.nlm.nih.gov/6803100
https://pubmed.ncbi.nlm.nih.gov/6803100
Autor:
J M, Gleisner, R L, Blakley
Publikováno v:
The Journal of biological chemistry. 250(4)
Carboxymethylation by iodoacetate of dihydrofolate reductase from the amethopterin-resistant mutant Streptococcus faecium var. Durans strain A leads to a loss of enzymic activity. Amino acid analysis showed that methionine is the only amino acid resi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dc83c94a2f18616213eed9e510201e0e
https://pubmed.ncbi.nlm.nih.gov/1112818
https://pubmed.ncbi.nlm.nih.gov/1112818
Publikováno v:
The Journal of surgical research. 41(6)
To test the hypothesis that the broad spectrum protease inhibitor, aprotinin, can prevent early pathophysiology of sepsis, we administered endotoxin (0.1-0.75 microgram/kg) by a 30-min infusion to awake goats. Animals were used as their own controls
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::284ff499527a516f50b5ed961ef2458c
https://pubmed.ncbi.nlm.nih.gov/2431222
https://pubmed.ncbi.nlm.nih.gov/2431222
Publikováno v:
Journal of applied physiology (Bethesda, Md. : 1985). 64(2)
Neutrophils have been implicated in the pathogenesis of acute lung injury associated with clinical and experimental sepsis. Data from in vitro systems and experimental animals have suggested that neutrophil-derived oxidants, particularly H2O2, may be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c66381e2f8b793e6e39f536461c7c923
https://pubmed.ncbi.nlm.nih.gov/3286599
https://pubmed.ncbi.nlm.nih.gov/3286599
Publikováno v:
The Journal of biological chemistry. 250(13)
The complete amino acid sequence of the mutant dihydrofolate reductase from Streptococcus faecium var. Durans strain A has been determined by sequence analysis of peptides produced by tryptic, chymotryptic, thermolytic, and mild acid cleavage of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::51e9c45044c32b34266a5b7962edad0c
https://pubmed.ncbi.nlm.nih.gov/1097435
https://pubmed.ncbi.nlm.nih.gov/1097435