Human protein Z

G. J. Broze; J. P. Miletich

doi:10.1172/JCI111317

Human protein Z

G. J. Broze, J. P. Miletich

Division of Hematology

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125 Scopus citations

Abstract

Protein Z was purified from human plasma by a four-step procedure which included barium citrate adsorption, ammonium sulfate fractionation, DEAE-Sepharose chromatography, and blue agarose chromatography with a yield of 20%. It is a 62,000 mol wt protein with an extinction coefficient of 12.0. The concentration of Protein Z in pooled, citrated plasma is 2.2 μg/ml and its half-life in patients starting warfarin anticoagulation therapy is estimated to be <2.5 d. The NH₂-terminal sequence is Ala-Gly-Ser-Tyr-Leu-Leu-(Gla)-(Gla)-Leu-Phe-(Gla)-Gly-Asn-Leu. Neither protein Z nor its cleavage products, which were obtained by treatment of Protein Z with thrombin or plasmin, incorporated [³H]diisopropyl fluorophosphate. The physiological function of Protein Z remains unknown.

Original language	English
Pages (from-to)	933-938
Number of pages	6
Journal	Journal of Clinical Investigation
Volume	73
Issue number	4
DOIs	https://doi.org/10.1172/JCI111317
State	Published - 1984

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title = "Human protein Z",

abstract = "Protein Z was purified from human plasma by a four-step procedure which included barium citrate adsorption, ammonium sulfate fractionation, DEAE-Sepharose chromatography, and blue agarose chromatography with a yield of 20%. It is a 62,000 mol wt protein with an extinction coefficient of 12.0. The concentration of Protein Z in pooled, citrated plasma is 2.2 μg/ml and its half-life in patients starting warfarin anticoagulation therapy is estimated to be <2.5 d. The NH2-terminal sequence is Ala-Gly-Ser-Tyr-Leu-Leu-(Gla)-(Gla)-Leu-Phe-(Gla)-Gly-Asn-Leu. Neither protein Z nor its cleavage products, which were obtained by treatment of Protein Z with thrombin or plasmin, incorporated [3H]diisopropyl fluorophosphate. The physiological function of Protein Z remains unknown.",

author = "Broze, {G. J.} and Miletich, {J. P.}",

year = "1984",

doi = "10.1172/JCI111317",

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volume = "73",

pages = "933--938",

journal = "Journal of Clinical Investigation",

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T1 - Human protein Z

AU - Broze, G. J.

AU - Miletich, J. P.

PY - 1984

Y1 - 1984

N2 - Protein Z was purified from human plasma by a four-step procedure which included barium citrate adsorption, ammonium sulfate fractionation, DEAE-Sepharose chromatography, and blue agarose chromatography with a yield of 20%. It is a 62,000 mol wt protein with an extinction coefficient of 12.0. The concentration of Protein Z in pooled, citrated plasma is 2.2 μg/ml and its half-life in patients starting warfarin anticoagulation therapy is estimated to be <2.5 d. The NH2-terminal sequence is Ala-Gly-Ser-Tyr-Leu-Leu-(Gla)-(Gla)-Leu-Phe-(Gla)-Gly-Asn-Leu. Neither protein Z nor its cleavage products, which were obtained by treatment of Protein Z with thrombin or plasmin, incorporated [3H]diisopropyl fluorophosphate. The physiological function of Protein Z remains unknown.

AB - Protein Z was purified from human plasma by a four-step procedure which included barium citrate adsorption, ammonium sulfate fractionation, DEAE-Sepharose chromatography, and blue agarose chromatography with a yield of 20%. It is a 62,000 mol wt protein with an extinction coefficient of 12.0. The concentration of Protein Z in pooled, citrated plasma is 2.2 μg/ml and its half-life in patients starting warfarin anticoagulation therapy is estimated to be <2.5 d. The NH2-terminal sequence is Ala-Gly-Ser-Tyr-Leu-Leu-(Gla)-(Gla)-Leu-Phe-(Gla)-Gly-Asn-Leu. Neither protein Z nor its cleavage products, which were obtained by treatment of Protein Z with thrombin or plasmin, incorporated [3H]diisopropyl fluorophosphate. The physiological function of Protein Z remains unknown.

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DO - 10.1172/JCI111317

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SN - 0021-9738

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SP - 933

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JO - Journal of Clinical Investigation

JF - Journal of Clinical Investigation

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Human protein Z

Abstract

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