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Giuseppe Specchia - One of the best experts on this subject based on the ideXlab platform.

  • Fibrinopeptide A excretion in urine A mArker of the cumulAtive thrombin Activity in stAble versus unstAble AnginA pAtients
    American Journal of Cardiology, 1991
    Co-Authors: Diego Ardissino, Maria Grazia Gamba, Piera Angelica Merlini, Alberto Rolla, Nicola Bruno, Gloria Demicheli, Paolo Barberis, Sophie Testa, Giuseppe Specchia
    Abstract:

    AbstrAct PlAsmA levels And 24-hour urine excretion of Fibrinopeptide A were meAsured in A consecutive series of 179 pAtients with AnginA pectoris. Sixty-four pAtients hAd stAble AnginA And 115 pAtients hAd unstAble AnginA. Urine wAs collected over 24 hours the dAy before coronAry ArteriogrAphy, And blood sAmples were tAken At the end of urine collection. When the vAlues of Fibrinopeptide A in plAsmA And in the 24-hour urine specimens were compAred, no significAnt correlAtion wAs found in pAtients with either stAble (rs = 0.16, difference not significAnt) And unstAble (rs = 0.07, difference not significAnt) AnginA. The concentrAtions of Fibrinopeptide A in the plAsmA did not differ significAntly when pAtients with stAble AnginA (rAnge 0.1 to 82.6, mediAn 7.4 ng/mL) were compAred with pAtients with unstAble AnginA (rAnge 0.2 to 61.7, mediAn 14 ng/mL, p = 0.055), whereAs Fibrinopeptide A 24-hour urinAry excretion wAs significAntly higher in pAtients with unstAble AnginA (rAnge 0.3 to 38.1, mediAn 11.8 μg/24 hr) thAn in pAtients with stAble AnginA (rAnge 0.4 to 38.1, mediAn 3.8 μg/24 hr, p

  • Fibrinopeptide A excretion in urine: A mArker of the cumulAtive thrombin Activity in stAble versus unstAble AnginA pAtients.
    The American journal of cardiology, 1991
    Co-Authors: Diego Ardissino, Maria Grazia Gamba, Piera Angelica Merlini, Alberto Rolla, Nicola Bruno, Gloria Demicheli, Paolo Barberis, Sophie Testa, Giuseppe Specchia
    Abstract:

    PlAsmA levels And 24-hour urine excretion of Fibrinopeptide A were meAsured in A consecutive series of 179 pAtients with AnginA pectoris. Sixty-four pAtients hAd stAble AnginA And 115 pAtients hAd unstAble AnginA. Urine wAs collected over 24 hours the dAy before coronAry ArteriogrAphy, And blood sAmples were tAken At the end of urine collection. When the vAlues of Fibrinopeptide A in plAsmA And in the 24-hour urine specimens were compAred, no significAnt correlAtion wAs found in pAtients with either stAble (rs = 0.16, difference not significAnt) And unstAble (rs = 0.07, difference not significAnt) AnginA. The concentrAtions of Fibrinopeptide A in the plAsmA did not differ significAntly when pAtients with stAble AnginA (rAnge 0.1 to 82.6, mediAn 7.4 ng/mL) were compAred with pAtients with unstAble AnginA (rAnge 0.2 to 61.7, mediAn 14 ng/mL, p = 0.055), whereAs Fibrinopeptide A 24-hour urinAry excretion wAs significAntly higher in pAtients with unstAble AnginA (rAnge 0.3 to 38.1, mediAn 11.8 microgrAms/24 hr) thAn in pAtients with stAble AnginA (rAnge 0.4 to 38.1, mediAn 3.8 microgrAms/24 hr, p less thAn 0.001). Twenty-four-hour urine excretion of Fibrinopeptide A in pAtients with unstAble AnginA And AngiogrAphicAlly documented intrAcoronAry thrombi were higher thAn the corresponding vAlues in pAtients with unstAble AnginA without such AngiogrAphic chArActeristic (p less thAn 0.001). The lArgest increAse in plAsmA And urine concentrAtion of Fibrinopeptide A wAs observed in pAtients whose first episode of AnginA At rest occurred within the previous 48 hours. We conclude thAt the cumulAtive thrombin Activity, Assessed by 24-hour urinAry excretion of Fibrinopeptide A, is A more useful index, compAred with single Fibrinopeptide A meAsurement in plAsmA, for discriminAting between pAtients with stAble And with unstAble AnginA pectoris.

David H Farrell - One of the best experts on this subject based on the ideXlab platform.

  • effects of impAired Fibrinopeptide A cleAvAge on fibrin clot structure studies with An Aα r16c dysfibrinogen
    Blood, 2006
    Co-Authors: Veronica H Flood, John W. Weisel, Chandrasekaran Nagaswami, Irina N Chernysh, Hamid Almondhiry, David H Farrell
    Abstract:

    CleAvAge of Fibrinopeptide A is the first step in fibrin clot formAtion, And mutAtions At the Fibrinopeptide A cleAvAge site Are the most common cAuse of dysfibrinogenemiA. We describe here the effect on clot structure of A mutAnt Aα R16C fibrinogen with defective Fibrinopeptide A cleAvAge (designAted fibrinogen Hershey III). The propositus, A young child with mild bleeding symptoms, wAs found to be heterozygous for the Aα R16C mutAtion. Fibrinogen wAs purified from Hershey III And control plAsmA viA glycine precipitAtion. Hershey III fibrinogen wAs only 63 ± 10% clottAble with thrombin (meAn ± SEM), As compAred to 96 ± 0.4% for normAl fibrinogen. Since the propositus wAs heterozygous for the mutAtion, the unclottAble portion likely consisted of mutAnt homodimers, but it wAs still possible thAt normAl/mutAnt heterodimers existed. BecAuse the cysteine in the mutAnt fibrinogen prevents thrombin-mediAted Fibrinopeptide A cleAvAge, we hypothesized thAt incorporAtion of uncleAved Fibrinopeptide A, if present, would Affect clot structure. Western blotting wAs used to evAluAte the presence of Fibrinopeptide A in clottAble And unclottAble fibrinogen. For fibrinogen Hershey III, both forms showed A substAntiAl Amount of Fibrinopeptide A, suggesting thAt mutAnt fibrinogen wAs incorporAted into the finAl clot. No Fibrinopeptide A wAs seen in either the clottAble or unclottAble fibrinogen from the normAl control. Next, fibrin clots were mAde with thrombin, criticAl-point dried, And visuAlized viA scAnning electron microscopy. Visco-elAstic meAsurements were obtAined with A torsion pendulum And clot permeAbility wAs compAred to thAt of clots formed with normAl fibrinogen. The relAtive proportions of normAl vs. mutAnt fibrinogen in the clottAble And unclottAble fibrinogen were Assessed by protein sequencing. ScAnning electron microscopy showed thAt the Hershey III clots displAyed AbnormAl Architecture with mAny short fibrin fibrils, consistent with premAture fibril terminAtion. Hershey III clots Also hAd thicker fibers, with An AverAge fiber diAmeter of 182 nm compAred to 151 nm for the normAl control. A significAnt difference in clot stiffness (G′), energy dissipAted by viscous processes (G″), And permeAbility (Ks) wAs seen when fibrinogen Hershey III wAs compAred to A normAl control (see tAble). Protein sequencing of the unclottAble Hershey III fibrinogen showed only the homozygous mutAnt form, while the fibrin clot showed ApproximAtely 50% eAch of the wild-type And mutAnt fibrinogen chAins. These results support the presence of both homodimers And heterodimers in fibrinogen Hershey III, And suggest thAt incorporAtion of Aα R16C heterodimers into the fibrin clot leAds to defects in fiber formAtion And clot structure. | | Hershey | III | Control | P | |:------------- | ------- | ----- | ------- | - | | G′ (dyne/cm2) | 10.8 | 37.9 | 0.03 | | | G″ (dyne/cm2) | 0.83 | 2.77 | 0.04 | | | TAn δ (G″/G′) | 0.077 | 0.076 | 0.79 | | | Ks (10−7 cm2) | 1.86 | 2.44 | 0.01 | | MechAnicAl Properties of Hershey III And Control Clots

  • effects of impAired Fibrinopeptide A cleAvAge on fibrin clot structure studies with An Aα r16c dysfibrinogen
    Blood, 2006
    Co-Authors: Veronica H Flood, John W. Weisel, Chandrasekaran Nagaswami, Irina N Chernysh, Hamid Almondhiry, David H Farrell
    Abstract:

    CleAvAge of Fibrinopeptide A is the first step in fibrin clot formAtion, And mutAtions At the Fibrinopeptide A cleAvAge site Are the most common cAuse of dysfibrinogenemiA. We describe here the effect on clot structure of A mutAnt Aα R16C fibrinogen with defective Fibrinopeptide A cleAvAge (designAted fibrinogen Hershey III). The propositus, A young child with mild bleeding symptoms, wAs found to be heterozygous for the Aα R16C mutAtion. Fibrinogen wAs purified from Hershey III And control plAsmA viA glycine precipitAtion. Hershey III fibrinogen wAs only 63 ± 10% clottAble with thrombin (meAn ± SEM), As compAred to 96 ± 0.4% for normAl fibrinogen. Since the propositus wAs heterozygous for the mutAtion, the unclottAble portion likely consisted of mutAnt homodimers, but it wAs still possible thAt normAl/mutAnt heterodimers existed. BecAuse the cysteine in the mutAnt fibrinogen prevents thrombin-mediAted Fibrinopeptide A cleAvAge, we hypothesized thAt incorporAtion of uncleAved Fibrinopeptide A, if present, would Affect clot structure. Western blotting wAs used to evAluAte the presence of Fibrinopeptide A in clottAble And unclottAble fibrinogen. For fibrinogen Hershey III, both forms showed A substAntiAl Amount of Fibrinopeptide A, suggesting thAt mutAnt fibrinogen wAs incorporAted into the finAl clot. No Fibrinopeptide A wAs seen in either the clottAble or unclottAble fibrinogen from the normAl control. Next, fibrin clots were mAde with thrombin, criticAl-point dried, And visuAlized viA scAnning electron microscopy. Visco-elAstic meAsurements were obtAined with A torsion pendulum And clot permeAbility wAs compAred to thAt of clots formed with normAl fibrinogen. The relAtive proportions of normAl vs. mutAnt fibrinogen in the clottAble And unclottAble fibrinogen were Assessed by protein sequencing. ScAnning electron microscopy showed thAt the Hershey III clots displAyed AbnormAl Architecture with mAny short fibrin fibrils, consistent with premAture fibril terminAtion. Hershey III clots Also hAd thicker fibers, with An AverAge fiber diAmeter of 182 nm compAred to 151 nm for the normAl control. A significAnt difference in clot stiffness (G′), energy dissipAted by viscous processes (G″), And permeAbility (Ks) wAs seen when fibrinogen Hershey III wAs compAred to A normAl control (see tAble). Protein sequencing of the unclottAble Hershey III fibrinogen showed only the homozygous mutAnt form, while the fibrin clot showed ApproximAtely 50% eAch of the wild-type And mutAnt fibrinogen chAins. These results support the presence of both homodimers And heterodimers in fibrinogen Hershey III, And suggest thAt incorporAtion of Aα R16C heterodimers into the fibrin clot leAds to defects in fiber formAtion And clot structure. | | Hershey | III | Control | P | |:------------- | ------- | ----- | ------- | - | | G′ (dyne/cm2) | 10.8 | 37.9 | 0.03 | | | G″ (dyne/cm2) | 0.83 | 2.77 | 0.04 | | | TAn δ (G″/G′) | 0.077 | 0.076 | 0.79 | | | Ks (10−7 cm2) | 1.86 | 2.44 | 0.01 | | MechAnicAl Properties of Hershey III And Control Clots

Masataka Arima - One of the best experts on this subject based on the ideXlab platform.

  • ElevAted Fibrinopeptide A (FPA) in PAtients with Lesch-NyhAn syndrome
    Brain & Development, 1992
    Co-Authors: Atsushi Imamura, Hideo Yamanouchi, Toru Kurokawa, Masataka Arima
    Abstract:

    The detection of elevAted Fibrinopeptide A (FPA) level in A pAtient with the Lesch-NyhAn syndrome complicAted with cerebrAl infArction prompted us to exAmine FPA level in 3 other pAtients with the syndrome. FPA level significAntly increAsed in All pAtients. Fibrinopeptide Bsl5-42 (FPBs15-42) level wAs increAsed in two, And both β-thromboglobulin (sTG) And plAtelet fActor 4 (PF4) levels were elevAted in one pAtient. These results suggest coAgulAtion AbnormAlities in pAtients with Lesch-NyhAn syndrome.

  • ElevAted Fibrinopeptide A (FP A) in PAtients with Lesch-NyhAn Syndrome
    1992
    Co-Authors: Atsushi Imamura, Hideo Yamanouchi, Toru Kurokawa, Masataka Arima
    Abstract:

    The detection of elevAted jibrinopeptide A (FPA) level in A pAtient with the Lesch-NyhAn syndrome complicAted with cerebrAl infArction prompted us to exAmine FPA level in 3 other pAtients with the syndrome. FPA level signijicAntly increAsed in All pAtients. Fibrinopeptide B{315-42 (FPB{315-42) level wAs increAsed in two, And both {3-thromboglobulin ({3TG) And plAtelet fActor 4 (PF4) levels were elevAted in one pAtient. These results suggest coAgulAtion AbnormAlities in pAtients with Lesch­ NyhAn syndrome. Key words: Fibrinopeptide A, Lesch­ NyhAn syndrome, coAgulAtion AbnormAlity.

Diego Ardissino - One of the best experts on this subject based on the ideXlab platform.

  • Fibrinopeptide A excretion in urine A mArker of the cumulAtive thrombin Activity in stAble versus unstAble AnginA pAtients
    American Journal of Cardiology, 1991
    Co-Authors: Diego Ardissino, Maria Grazia Gamba, Piera Angelica Merlini, Alberto Rolla, Nicola Bruno, Gloria Demicheli, Paolo Barberis, Sophie Testa, Giuseppe Specchia
    Abstract:

    AbstrAct PlAsmA levels And 24-hour urine excretion of Fibrinopeptide A were meAsured in A consecutive series of 179 pAtients with AnginA pectoris. Sixty-four pAtients hAd stAble AnginA And 115 pAtients hAd unstAble AnginA. Urine wAs collected over 24 hours the dAy before coronAry ArteriogrAphy, And blood sAmples were tAken At the end of urine collection. When the vAlues of Fibrinopeptide A in plAsmA And in the 24-hour urine specimens were compAred, no significAnt correlAtion wAs found in pAtients with either stAble (rs = 0.16, difference not significAnt) And unstAble (rs = 0.07, difference not significAnt) AnginA. The concentrAtions of Fibrinopeptide A in the plAsmA did not differ significAntly when pAtients with stAble AnginA (rAnge 0.1 to 82.6, mediAn 7.4 ng/mL) were compAred with pAtients with unstAble AnginA (rAnge 0.2 to 61.7, mediAn 14 ng/mL, p = 0.055), whereAs Fibrinopeptide A 24-hour urinAry excretion wAs significAntly higher in pAtients with unstAble AnginA (rAnge 0.3 to 38.1, mediAn 11.8 μg/24 hr) thAn in pAtients with stAble AnginA (rAnge 0.4 to 38.1, mediAn 3.8 μg/24 hr, p

  • Fibrinopeptide A excretion in urine: A mArker of the cumulAtive thrombin Activity in stAble versus unstAble AnginA pAtients.
    The American journal of cardiology, 1991
    Co-Authors: Diego Ardissino, Maria Grazia Gamba, Piera Angelica Merlini, Alberto Rolla, Nicola Bruno, Gloria Demicheli, Paolo Barberis, Sophie Testa, Giuseppe Specchia
    Abstract:

    PlAsmA levels And 24-hour urine excretion of Fibrinopeptide A were meAsured in A consecutive series of 179 pAtients with AnginA pectoris. Sixty-four pAtients hAd stAble AnginA And 115 pAtients hAd unstAble AnginA. Urine wAs collected over 24 hours the dAy before coronAry ArteriogrAphy, And blood sAmples were tAken At the end of urine collection. When the vAlues of Fibrinopeptide A in plAsmA And in the 24-hour urine specimens were compAred, no significAnt correlAtion wAs found in pAtients with either stAble (rs = 0.16, difference not significAnt) And unstAble (rs = 0.07, difference not significAnt) AnginA. The concentrAtions of Fibrinopeptide A in the plAsmA did not differ significAntly when pAtients with stAble AnginA (rAnge 0.1 to 82.6, mediAn 7.4 ng/mL) were compAred with pAtients with unstAble AnginA (rAnge 0.2 to 61.7, mediAn 14 ng/mL, p = 0.055), whereAs Fibrinopeptide A 24-hour urinAry excretion wAs significAntly higher in pAtients with unstAble AnginA (rAnge 0.3 to 38.1, mediAn 11.8 microgrAms/24 hr) thAn in pAtients with stAble AnginA (rAnge 0.4 to 38.1, mediAn 3.8 microgrAms/24 hr, p less thAn 0.001). Twenty-four-hour urine excretion of Fibrinopeptide A in pAtients with unstAble AnginA And AngiogrAphicAlly documented intrAcoronAry thrombi were higher thAn the corresponding vAlues in pAtients with unstAble AnginA without such AngiogrAphic chArActeristic (p less thAn 0.001). The lArgest increAse in plAsmA And urine concentrAtion of Fibrinopeptide A wAs observed in pAtients whose first episode of AnginA At rest occurred within the previous 48 hours. We conclude thAt the cumulAtive thrombin Activity, Assessed by 24-hour urinAry excretion of Fibrinopeptide A, is A more useful index, compAred with single Fibrinopeptide A meAsurement in plAsmA, for discriminAting between pAtients with stAble And with unstAble AnginA pectoris.

Veronica H Flood - One of the best experts on this subject based on the ideXlab platform.

  • effects of impAired Fibrinopeptide A cleAvAge on fibrin clot structure studies with An Aα r16c dysfibrinogen
    Blood, 2006
    Co-Authors: Veronica H Flood, John W. Weisel, Chandrasekaran Nagaswami, Irina N Chernysh, Hamid Almondhiry, David H Farrell
    Abstract:

    CleAvAge of Fibrinopeptide A is the first step in fibrin clot formAtion, And mutAtions At the Fibrinopeptide A cleAvAge site Are the most common cAuse of dysfibrinogenemiA. We describe here the effect on clot structure of A mutAnt Aα R16C fibrinogen with defective Fibrinopeptide A cleAvAge (designAted fibrinogen Hershey III). The propositus, A young child with mild bleeding symptoms, wAs found to be heterozygous for the Aα R16C mutAtion. Fibrinogen wAs purified from Hershey III And control plAsmA viA glycine precipitAtion. Hershey III fibrinogen wAs only 63 ± 10% clottAble with thrombin (meAn ± SEM), As compAred to 96 ± 0.4% for normAl fibrinogen. Since the propositus wAs heterozygous for the mutAtion, the unclottAble portion likely consisted of mutAnt homodimers, but it wAs still possible thAt normAl/mutAnt heterodimers existed. BecAuse the cysteine in the mutAnt fibrinogen prevents thrombin-mediAted Fibrinopeptide A cleAvAge, we hypothesized thAt incorporAtion of uncleAved Fibrinopeptide A, if present, would Affect clot structure. Western blotting wAs used to evAluAte the presence of Fibrinopeptide A in clottAble And unclottAble fibrinogen. For fibrinogen Hershey III, both forms showed A substAntiAl Amount of Fibrinopeptide A, suggesting thAt mutAnt fibrinogen wAs incorporAted into the finAl clot. No Fibrinopeptide A wAs seen in either the clottAble or unclottAble fibrinogen from the normAl control. Next, fibrin clots were mAde with thrombin, criticAl-point dried, And visuAlized viA scAnning electron microscopy. Visco-elAstic meAsurements were obtAined with A torsion pendulum And clot permeAbility wAs compAred to thAt of clots formed with normAl fibrinogen. The relAtive proportions of normAl vs. mutAnt fibrinogen in the clottAble And unclottAble fibrinogen were Assessed by protein sequencing. ScAnning electron microscopy showed thAt the Hershey III clots displAyed AbnormAl Architecture with mAny short fibrin fibrils, consistent with premAture fibril terminAtion. Hershey III clots Also hAd thicker fibers, with An AverAge fiber diAmeter of 182 nm compAred to 151 nm for the normAl control. A significAnt difference in clot stiffness (G′), energy dissipAted by viscous processes (G″), And permeAbility (Ks) wAs seen when fibrinogen Hershey III wAs compAred to A normAl control (see tAble). Protein sequencing of the unclottAble Hershey III fibrinogen showed only the homozygous mutAnt form, while the fibrin clot showed ApproximAtely 50% eAch of the wild-type And mutAnt fibrinogen chAins. These results support the presence of both homodimers And heterodimers in fibrinogen Hershey III, And suggest thAt incorporAtion of Aα R16C heterodimers into the fibrin clot leAds to defects in fiber formAtion And clot structure. | | Hershey | III | Control | P | |:------------- | ------- | ----- | ------- | - | | G′ (dyne/cm2) | 10.8 | 37.9 | 0.03 | | | G″ (dyne/cm2) | 0.83 | 2.77 | 0.04 | | | TAn δ (G″/G′) | 0.077 | 0.076 | 0.79 | | | Ks (10−7 cm2) | 1.86 | 2.44 | 0.01 | | MechAnicAl Properties of Hershey III And Control Clots

  • effects of impAired Fibrinopeptide A cleAvAge on fibrin clot structure studies with An Aα r16c dysfibrinogen
    Blood, 2006
    Co-Authors: Veronica H Flood, John W. Weisel, Chandrasekaran Nagaswami, Irina N Chernysh, Hamid Almondhiry, David H Farrell
    Abstract:

    CleAvAge of Fibrinopeptide A is the first step in fibrin clot formAtion, And mutAtions At the Fibrinopeptide A cleAvAge site Are the most common cAuse of dysfibrinogenemiA. We describe here the effect on clot structure of A mutAnt Aα R16C fibrinogen with defective Fibrinopeptide A cleAvAge (designAted fibrinogen Hershey III). The propositus, A young child with mild bleeding symptoms, wAs found to be heterozygous for the Aα R16C mutAtion. Fibrinogen wAs purified from Hershey III And control plAsmA viA glycine precipitAtion. Hershey III fibrinogen wAs only 63 ± 10% clottAble with thrombin (meAn ± SEM), As compAred to 96 ± 0.4% for normAl fibrinogen. Since the propositus wAs heterozygous for the mutAtion, the unclottAble portion likely consisted of mutAnt homodimers, but it wAs still possible thAt normAl/mutAnt heterodimers existed. BecAuse the cysteine in the mutAnt fibrinogen prevents thrombin-mediAted Fibrinopeptide A cleAvAge, we hypothesized thAt incorporAtion of uncleAved Fibrinopeptide A, if present, would Affect clot structure. Western blotting wAs used to evAluAte the presence of Fibrinopeptide A in clottAble And unclottAble fibrinogen. For fibrinogen Hershey III, both forms showed A substAntiAl Amount of Fibrinopeptide A, suggesting thAt mutAnt fibrinogen wAs incorporAted into the finAl clot. No Fibrinopeptide A wAs seen in either the clottAble or unclottAble fibrinogen from the normAl control. Next, fibrin clots were mAde with thrombin, criticAl-point dried, And visuAlized viA scAnning electron microscopy. Visco-elAstic meAsurements were obtAined with A torsion pendulum And clot permeAbility wAs compAred to thAt of clots formed with normAl fibrinogen. The relAtive proportions of normAl vs. mutAnt fibrinogen in the clottAble And unclottAble fibrinogen were Assessed by protein sequencing. ScAnning electron microscopy showed thAt the Hershey III clots displAyed AbnormAl Architecture with mAny short fibrin fibrils, consistent with premAture fibril terminAtion. Hershey III clots Also hAd thicker fibers, with An AverAge fiber diAmeter of 182 nm compAred to 151 nm for the normAl control. A significAnt difference in clot stiffness (G′), energy dissipAted by viscous processes (G″), And permeAbility (Ks) wAs seen when fibrinogen Hershey III wAs compAred to A normAl control (see tAble). Protein sequencing of the unclottAble Hershey III fibrinogen showed only the homozygous mutAnt form, while the fibrin clot showed ApproximAtely 50% eAch of the wild-type And mutAnt fibrinogen chAins. These results support the presence of both homodimers And heterodimers in fibrinogen Hershey III, And suggest thAt incorporAtion of Aα R16C heterodimers into the fibrin clot leAds to defects in fiber formAtion And clot structure. | | Hershey | III | Control | P | |:------------- | ------- | ----- | ------- | - | | G′ (dyne/cm2) | 10.8 | 37.9 | 0.03 | | | G″ (dyne/cm2) | 0.83 | 2.77 | 0.04 | | | TAn δ (G″/G′) | 0.077 | 0.076 | 0.79 | | | Ks (10−7 cm2) | 1.86 | 2.44 | 0.01 | | MechAnicAl Properties of Hershey III And Control Clots