Abstract
A reproducible procedure for the isolation, from human placenta, of a cathepsin B1 in a homogeneous state, demonstrated by electrophoretic, ultracentrifugal and enzymic criteria, was carried out. The pH optimum was near pH5.5. The placental enzyme catalysed the release of acid-soluble u.v.-dense products from haemoglobin and myoglobin. It was inhibited by heavy metals and several compounds which react with the thiol groups. The optimum temperature was between 37 degrees and 42 degrees C. The molecular weight of the enzyme was calculated to be 24250.
MeSH Terms
Cathepsins/antagonists & inhibitors,isolation & purification,metabolism
Cations, Divalent
Chromatography, DEAE-Cellulose
Chromatography, Gel
Chromatography, Ion Exchange
Electrophoresis, Disc
Enzyme Activation
Female
Hemoglobins
Humans
Hydrogen-Ion Concentration
Kinetics
Molecular Weight
Myoglobin
Placenta/enzymology
Pregnancy
Spectrophotometry, Ultraviolet
Sulfhydryl Reagents/pharmacology
Temperature
Ultracentrifugation
Ultrafiltration
Chemicals
Cations, Divalent
Hemoglobins
Myoglobin
Sulfhydryl Reagents
Cathepsins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Swanson A A
Martin B J
Spicer S S
References (14)
14 references, click to expand
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