Characterization of overt carnitine palmitoyltransferase in rat platelets; involvement of insulin on its regulation
Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubatio...
Ausführliche Beschreibung
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Englisch |
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1991 |
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8 |
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Springer Online Journal Archives 1860-2002 |
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Übergeordnetes Werk: |
in: Molecular and cellular biochemistry - 1973, 103(1991) vom: Jan., Seite 23-30 |
Übergeordnetes Werk: |
volume:103 ; year:1991 ; month:01 ; pages:23-30 ; extent:8 |
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NLEJ198042469 |
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520 | |a Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver. | ||
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(DE-627)NLEJ198042469 DE-627 ger DE-627 rakwb eng Characterization of overt carnitine palmitoyltransferase in rat platelets; involvement of insulin on its regulation 1991 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver. Springer Online Journal Archives 1860-2002 Iida, Reimi oth Takeyama, Naoshi oth Iida, Naohiro oth Tanaka, Takaya oth in Molecular and cellular biochemistry 1973 103(1991) vom: Jan., Seite 23-30 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:103 year:1991 month:01 pages:23-30 extent:8 http://dx.doi.org/10.1007/BF00229590 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 103 1991 1 23-30 8 |
spelling |
(DE-627)NLEJ198042469 DE-627 ger DE-627 rakwb eng Characterization of overt carnitine palmitoyltransferase in rat platelets; involvement of insulin on its regulation 1991 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver. Springer Online Journal Archives 1860-2002 Iida, Reimi oth Takeyama, Naoshi oth Iida, Naohiro oth Tanaka, Takaya oth in Molecular and cellular biochemistry 1973 103(1991) vom: Jan., Seite 23-30 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:103 year:1991 month:01 pages:23-30 extent:8 http://dx.doi.org/10.1007/BF00229590 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 103 1991 1 23-30 8 |
allfields_unstemmed |
(DE-627)NLEJ198042469 DE-627 ger DE-627 rakwb eng Characterization of overt carnitine palmitoyltransferase in rat platelets; involvement of insulin on its regulation 1991 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver. Springer Online Journal Archives 1860-2002 Iida, Reimi oth Takeyama, Naoshi oth Iida, Naohiro oth Tanaka, Takaya oth in Molecular and cellular biochemistry 1973 103(1991) vom: Jan., Seite 23-30 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:103 year:1991 month:01 pages:23-30 extent:8 http://dx.doi.org/10.1007/BF00229590 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 103 1991 1 23-30 8 |
allfieldsGer |
(DE-627)NLEJ198042469 DE-627 ger DE-627 rakwb eng Characterization of overt carnitine palmitoyltransferase in rat platelets; involvement of insulin on its regulation 1991 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver. Springer Online Journal Archives 1860-2002 Iida, Reimi oth Takeyama, Naoshi oth Iida, Naohiro oth Tanaka, Takaya oth in Molecular and cellular biochemistry 1973 103(1991) vom: Jan., Seite 23-30 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:103 year:1991 month:01 pages:23-30 extent:8 http://dx.doi.org/10.1007/BF00229590 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 103 1991 1 23-30 8 |
allfieldsSound |
(DE-627)NLEJ198042469 DE-627 ger DE-627 rakwb eng Characterization of overt carnitine palmitoyltransferase in rat platelets; involvement of insulin on its regulation 1991 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver. Springer Online Journal Archives 1860-2002 Iida, Reimi oth Takeyama, Naoshi oth Iida, Naohiro oth Tanaka, Takaya oth in Molecular and cellular biochemistry 1973 103(1991) vom: Jan., Seite 23-30 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:103 year:1991 month:01 pages:23-30 extent:8 http://dx.doi.org/10.1007/BF00229590 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 103 1991 1 23-30 8 |
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characterization of overt carnitine palmitoyltransferase in rat platelets; involvement of insulin on its regulation |
title_auth |
Characterization of overt carnitine palmitoyltransferase in rat platelets; involvement of insulin on its regulation |
abstract |
Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver. |
abstractGer |
Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver. |
abstract_unstemmed |
Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ198042469</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210705231929.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070527s1991 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ198042469</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Characterization of overt carnitine palmitoyltransferase in rat platelets; involvement of insulin on its regulation</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1991</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">8</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Summary Saponin-permeabilization (30 µg/ml) of the platelet plasma membrane, which enables access of added compounds to mitochondrial overt carnitine palmitoyltransferase (CPT I), was applied to allow the rapid determination of CPT I activity in situ. The effects of diabetes and short-term incubation with insulin in vitro on the kinetic parameters and malonyl-CoA sensitivity of CPT I were also studied in rat platelets. CPT I exhibited ordinary Michaelis-Menten kinetics when platelets were incubated with palmitoyl-CoA. Malonyl-CoA showed an I50 (concentration giving 50% inhibition of CPT activity) of 0.92 ± 0.11 µM in permeabilized platelets. Platelets obtained from diabetic rats (induced by streptozotocin injection) exhibited an increased Vmax. and I50 for malonyl-CoA, and an unaltered Km for palmitoyl-CoA. In contrast, preincubation of platelets prepared from both fed control rats and diabetic rats with insulin (100 and 150 µ-cU/ml) led to a decrease in enzyme activity when assayed with 75 µM palmitoyl-CoA and 0.5 mM L-carnitine as substrates. These in vivo and in vitro results suggested that insulin directly modulated rat platelet CPT I activity, as it does in the liver.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Iida, Reimi</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Takeyama, Naoshi</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Iida, Naohiro</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tanaka, Takaya</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Molecular and cellular biochemistry</subfield><subfield code="d">1973</subfield><subfield code="g">103(1991) vom: Jan., Seite 23-30</subfield><subfield code="w">(DE-627)NLEJ188989099</subfield><subfield code="w">(DE-600)2003615-2</subfield><subfield code="x">1573-4919</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:103</subfield><subfield code="g">year:1991</subfield><subfield code="g">month:01</subfield><subfield code="g">pages:23-30</subfield><subfield code="g">extent:8</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/BF00229590</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">103</subfield><subfield code="j">1991</subfield><subfield code="c">1</subfield><subfield code="h">23-30</subfield><subfield code="g">8</subfield></datafield></record></collection>
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