Characterization of proteolytic systems in human and rat urine

Uri Wormser; Gerhard Zbinden

doi:10.1016/S0006-291X(85)80143-1

Characterization of proteolytic systems in human and rat urine

Uri Wormser^*, Gerhard Zbinden

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Activities of proteolytic enzymes were detected in rat and human urine by using [¹²⁵I]iodo-insulin B chain as a substrate. The pH optimum of human urine activity was in the acidic range (pH 2.0) whereas the rat urine had two pH optima, one at the acidic range similar to human urine and another at pH 7.5. The activities were linear with time and amount of enzyme. Study with various proteinase inhibitors revealed that the acidic pH activities of human and rat urine were apparently of carboxyl endopeptidases since they were totally inhibited by pepstatin 10^-8M. The neutral pH proteolysis of rat urine was inhibited by chelating agents and therefore it was considered as a metalloendopeptidase activity. These findings show the difference between the content of urinary proteolytic enzymes in humans and in rats by using a sensitive and simple radioactive assay.

Original language	English
Pages (from-to)	191-197
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	127
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(85)80143-1
State	Published - 28 Feb 1985
Externally published	Yes

Access to Document

10.1016/S0006-291X(85)80143-1

Cite this

@article{562e8b09c89248c0b41fdd911603d1f6,

title = "Characterization of proteolytic systems in human and rat urine",

abstract = "Activities of proteolytic enzymes were detected in rat and human urine by using [125I]iodo-insulin B chain as a substrate. The pH optimum of human urine activity was in the acidic range (pH 2.0) whereas the rat urine had two pH optima, one at the acidic range similar to human urine and another at pH 7.5. The activities were linear with time and amount of enzyme. Study with various proteinase inhibitors revealed that the acidic pH activities of human and rat urine were apparently of carboxyl endopeptidases since they were totally inhibited by pepstatin 10-8M. The neutral pH proteolysis of rat urine was inhibited by chelating agents and therefore it was considered as a metalloendopeptidase activity. These findings show the difference between the content of urinary proteolytic enzymes in humans and in rats by using a sensitive and simple radioactive assay.",

author = "Uri Wormser and Gerhard Zbinden",

year = "1985",

month = feb,

day = "28",

doi = "10.1016/S0006-291X(85)80143-1",

language = "אנגלית",

volume = "127",

pages = "191--197",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "1",

}

TY - JOUR

T1 - Characterization of proteolytic systems in human and rat urine

AU - Wormser, Uri

AU - Zbinden, Gerhard

PY - 1985/2/28

Y1 - 1985/2/28

N2 - Activities of proteolytic enzymes were detected in rat and human urine by using [125I]iodo-insulin B chain as a substrate. The pH optimum of human urine activity was in the acidic range (pH 2.0) whereas the rat urine had two pH optima, one at the acidic range similar to human urine and another at pH 7.5. The activities were linear with time and amount of enzyme. Study with various proteinase inhibitors revealed that the acidic pH activities of human and rat urine were apparently of carboxyl endopeptidases since they were totally inhibited by pepstatin 10-8M. The neutral pH proteolysis of rat urine was inhibited by chelating agents and therefore it was considered as a metalloendopeptidase activity. These findings show the difference between the content of urinary proteolytic enzymes in humans and in rats by using a sensitive and simple radioactive assay.

AB - Activities of proteolytic enzymes were detected in rat and human urine by using [125I]iodo-insulin B chain as a substrate. The pH optimum of human urine activity was in the acidic range (pH 2.0) whereas the rat urine had two pH optima, one at the acidic range similar to human urine and another at pH 7.5. The activities were linear with time and amount of enzyme. Study with various proteinase inhibitors revealed that the acidic pH activities of human and rat urine were apparently of carboxyl endopeptidases since they were totally inhibited by pepstatin 10-8M. The neutral pH proteolysis of rat urine was inhibited by chelating agents and therefore it was considered as a metalloendopeptidase activity. These findings show the difference between the content of urinary proteolytic enzymes in humans and in rats by using a sensitive and simple radioactive assay.

UR - http://www.scopus.com/inward/record.url?scp=0021982023&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(85)80143-1

DO - 10.1016/S0006-291X(85)80143-1

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

C2 - 3919724

AN - SCOPUS:0021982023

SN - 0006-291X

VL - 127

SP - 191

EP - 197

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Characterization of proteolytic systems in human and rat urine

Abstract

Access to Document

Other files and links

Fingerprint

Cite this