Zobrazeno 1 - 5
of 5
pro vyhledávání: '"G. M. Lindenbaum"'
Autor:
G. M. Lindenbaum, Moskvichev Bv, I. Z. Konshina, L. V. Makhovenko, A. P. Kashkin, I. M. Tereshin
Publikováno v:
Pharmaceutical Chemistry Journal. 12:844-848
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::65eee6ab978f21b3dab475bb459207ae
https://doi.org/10.1007/bf00777623
https://doi.org/10.1007/bf00777623
Publikováno v:
Pharmaceutical Chemistry Journal. 11:806-809
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c004fa9085c20e6b5b261e9b362d3e2c
https://doi.org/10.1007/bf00779300
https://doi.org/10.1007/bf00779300
Publikováno v:
Pharmaceutical Chemistry Journal. 11:955-959
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::44441afbba2ed23a700f57e70b65a0ee
https://doi.org/10.1007/bf00778026
https://doi.org/10.1007/bf00778026
Autor:
G M, Lindenbaum, I M, Tereshin
Publikováno v:
Biokhimiia (Moscow, Russia). 43(12)
Interactions between native terrylytin and trypsin and their derivatives modified by water-soluble dextrans on one hand and human blood serum inhibitors on the other, were studied. It was shown that modification of the enzymes results in changes in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cdb26524db7caa32b214bc249df032b4
https://pubmed.ncbi.nlm.nih.gov/84689
https://pubmed.ncbi.nlm.nih.gov/84689
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 13(5)
The molecular weight distribution, thermal stability during autolysis, resistance to human serum inhibitors as well as temperature optimum of native and dextran-modified trypsin were investigated. The seeming constants of autolytic inactivation and i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b2b5ea67a8be2e5c97d241064612c18c
https://pubmed.ncbi.nlm.nih.gov/918022
https://pubmed.ncbi.nlm.nih.gov/918022