Linked Life Data

1200704

Source:http://linkedlifedata.com/resource/pubmed/id/1200704

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1976-2-9
pubmed:abstractText
Two alkaline proteases, one splitting preferentially the substrates of chymotrypsin (ATEE) and the other one those of trypsin (BAEE), were separated and partially purified by chromatographic means from human skin extract made in a buffer containing 1.07 mol/1 KC1. The proteins soluble in dilute buffer were removed by a prior extraction. The enzymes could be separated effectively only in the presence of KC1 at a high conc-ntration since large molecular size aggregates or polymers were formed in solutions of low ionic strength. In the presence of 2 mol/1 KC1 the molecular size of the BAEE-hydrolysing enzyme was 120000 and that of the ATEE-hydrolysing enzyme 30000. The ATEE-hydrolysing enzyme was purified by Sephadex G-100 gel filtration and DEAE-cellulose chromatography about 250 fold. It also hydrolysed esters of tryptophane and phenylalanine as well as casein with optimum pH 7.8--8.2. The enzyme was inhibited effectively by LBTI, SBTI and partially by trasylol, TPCK and TLCK, but not by E-600 and SH-modifers. The hydrolysis of ATEE was doubled in the presence of 1 mol/lKCl, NaCl, KBr or NaBr but that of casein was inhibited to some extent. Human serum and alpha-1-antitrypsin inhibited this enzyme but not C1-inactivator. alpha-2-Macroglobulin did not protect if from inhibition by SBTI. The BAEE-hydrolysing enzyme was purified by Sephadex G-100 gel filtration and hydroxylapatite chromatography about 30 fold. It also split other esters of substituted basic amino acids as well as BAPA and histone proteins with optimum pH 7.5--8.2. It was inhibited by Trasylol and TLCK, but not by LBTI, SBTI, OMTI, TPCK, E-600, SH-modifiers, human serum, C1-inactivator or alpha-1-antitrypsin. Neither of these enzymes is exactly similar to any one of the enzymes so far separated from human tissues or fluids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0340-3696
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
261-76
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Human skin proteases: separation and characterization of two alkaline proteases, one splitting trypsin and the other chymotrypsin substrates.
pubmed:publicationType
Journal Article