Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-11-13
pubmed:abstractText
An extracellular alkaline serine proteinase from Thermus strain ToK3 was isolated and purified to homogeneity by (NH4)2SO4 precipitation followed by ion-exchange chromatography on DEAE-cellulose and QAE-Sephadex, affinity chromatography on N alpha-benzyloxycarbonyl-D-phenylalanyl-triethylenetetraminyl-Sepha rose 4B and gel-filtration chromatography on Sephadex G-75. The purified enzyme had a pI of 8.9 and an Mr determined by gel-permeation chromatography of 25,000. The specific activity was about 37,700 proteolytic units/mg with casein as substrate, and the pH optimum was 9.5. Proteolytic activity was inhibited by low concentrations of di-isopropyl phosphorofluoridate and phenylmethanesulphonyl fluoride, but was unaffected by EDTA, EGTA, o-phenanthroline, N-ethyl-5-phenylisoxazolium-3'-sulphonate, N alpha-p-tosyl-L-phenylalanylchloromethane, N alpha-p-tosyl-L-lysylchloromethane, trypsin inhibitors and pepstatin A. The enzyme contained approx. 10% carbohydrate and four disulphide bonds. No Ca2+, Zn2+ or free thiol groups were detected. It hydrolysed several native and dye-linked proteins and synthetic chromogenic peptides and esters. The enzyme was very thermostable (half-life values were 840 min at 80 degrees C, 45 min at 90 degrees C and 5 min at 100 degrees C). The enzyme was unstable at low ionic strength: after 60 min at 75 degrees C in 0.1 M-Tris/acetate buffer, pH 8, only 20% activity remained, compared with no loss in 0.1 M-Tris/acetate buffer, pH 8, containing 0.4 M-NaCl.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-1172386, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-1182109, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-166995, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-16866, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-3114022, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-3120701, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-4177067, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-4208643, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-4578954, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-4584800, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-5003986, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-5025356, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-5114933, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-5528242, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-603028, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-6341371, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-6363390, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-6383347, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-6400480, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-6408058, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-6750031, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-6751397, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-6758705, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-6855573, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-7459341, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-814920, http://linkedlifedata.com/resource/pubmed/commentcorrection/2803259-911794
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
409-16
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Caldolase, a chelator-insensitive extracellular serine proteinase from a Thermus spp.
pubmed:affiliation
Thermophile Research Group, School of Science, University of Waikato, Hamilton, New Zealand.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't