Abstract：
:Kallikrein was purified from horse kidney by several steps of chromatographic procedure and by affinity chromatography on Sepharose-Concanavaline. Horse urinary kallikrein was previously purified by DE-32 hydroxylapatite and by Sephadex G-100 gel filtration. On the purified final sample of renal and urinary kallikrein the aminoacid composition and the gel electrophoretic molecular weight were determined. The ratio in micronMoles between each aminoacid residue of both hydrolyzed renal and urinary kallikrein of horse is about 1,00 +/- 0,30. Except for Pro, 1/2 Cys and basic aminoacid residues a good proportion was obtained. It is confirmed that the different molecular weight, respectively 47,500 for renal kallikrein and 28,000 for the urinary enzyme is an artefact of the different procedures used for the purification of horse kallikrein.
journal_name
Adv Exp Med Bioljournal_title
Advances in experimental medicine and biologyauthors
Porcelli G,Marini-Bettolo GB,Croxatto HR,Di Jorio Mdoi
10.1007/978-1-4757-0926-1_31subject
Has Abstractpub_date
1979-01-01 00:00:00pages
325-33eissn
0065-2598issn
2214-8019journal_volume
120Apub_type
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