A family of protein growth curves with extension to other chemical body components together with application to animal nutrition and improvement
Theory that successfully explains the magnitude and range of estimates of protein retention (PR) efficiency from the cost of turnover of existing protein indicates that conventional curves for growth description are inappropriate for protein growth. A solution to this problem is found in the conside...
Ausführliche Beschreibung
Autor*in: |
C.Z. Roux [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2011 |
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Schlagwörter: |
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Übergeordnetes Werk: |
In: Animal - Elsevier, 2021, 5(2011), 3, Seite 439-449 |
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Übergeordnetes Werk: |
volume:5 ; year:2011 ; number:3 ; pages:439-449 |
Links: |
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DOI / URN: |
10.1017/S1751731110001874 |
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Katalog-ID: |
DOAJ05654281X |
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520 | |a Theory that successfully explains the magnitude and range of estimates of protein retention (PR) efficiency from the cost of turnover of existing protein indicates that conventional curves for growth description are inappropriate for protein growth. A solution to this problem is found in the consideration that the rate-limiting steps for protein synthesis (PS) and breakdown are likely to be associated with the diffusion of metabolites in and between cells. The algebraic scaling of nuclear and cellular diffusion capacity with tissue or total body protein leads to a parameterization of the primal differential equation for PR (kg/day) based on two terms representing PS and breakdown, viz. PR = cQ[(P/α)X + Z - (4/9)Y — (P/α)X + Z]. where c is an arbitrary constant, Q is the proportion of nuclei active in cell growth or division in a tissue or the whole body, α is the limit mass for protein (P, kg) in a tissue or the whole body, the power X + Z represents the rate-limiting steps in protein breakdown and Y is the power of the relationship between cell volume and the amount of tissue protein. For the whole body, the contribution of the different tissues should be weighted in proportion to their PS rates with, on average, Y = 1/2. The constant 4/9 arises from the scaling of the specific diffusion rate of DNA activator precursors from nuclear dimensions and from the relationship between nuclear and cell volume. Experimental evidence on protein breakdown rate as well as protein and body mass points of inflection indicates that the range of theoretically possible numerical values of the rate-limiting powers X + Z = (i + 3)/9 for i = 1, 2, …,12 seems adequate for the description of the range of observed whole body protein and body mass growth patterns for mammals. Q = 1 represents maximal protein retention, and for 0 < Q < 1, experimental evidence exists in support of a theoretical relationship between Q and food ingestion. The conclusion follows that some knowledge of the protein limit mass (α) and of the point of inflection (related to X + Z) is the main requirement for the application of the theory for description and prediction in animal nutrition and breeding. | ||
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10.1017/S1751731110001874 doi (DE-627)DOAJ05654281X (DE-599)DOAJ7b6bdf01ddb640cb813905b2f448d0b1 DE-627 ger DE-627 rakwb eng SF1-1100 C.Z. Roux verfasserin aut A family of protein growth curves with extension to other chemical body components together with application to animal nutrition and improvement 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Theory that successfully explains the magnitude and range of estimates of protein retention (PR) efficiency from the cost of turnover of existing protein indicates that conventional curves for growth description are inappropriate for protein growth. A solution to this problem is found in the consideration that the rate-limiting steps for protein synthesis (PS) and breakdown are likely to be associated with the diffusion of metabolites in and between cells. The algebraic scaling of nuclear and cellular diffusion capacity with tissue or total body protein leads to a parameterization of the primal differential equation for PR (kg/day) based on two terms representing PS and breakdown, viz. PR = cQ[(P/α)X + Z - (4/9)Y — (P/α)X + Z]. where c is an arbitrary constant, Q is the proportion of nuclei active in cell growth or division in a tissue or the whole body, α is the limit mass for protein (P, kg) in a tissue or the whole body, the power X + Z represents the rate-limiting steps in protein breakdown and Y is the power of the relationship between cell volume and the amount of tissue protein. For the whole body, the contribution of the different tissues should be weighted in proportion to their PS rates with, on average, Y = 1/2. The constant 4/9 arises from the scaling of the specific diffusion rate of DNA activator precursors from nuclear dimensions and from the relationship between nuclear and cell volume. Experimental evidence on protein breakdown rate as well as protein and body mass points of inflection indicates that the range of theoretically possible numerical values of the rate-limiting powers X + Z = (i + 3)/9 for i = 1, 2, …,12 seems adequate for the description of the range of observed whole body protein and body mass growth patterns for mammals. Q = 1 represents maximal protein retention, and for 0 < Q < 1, experimental evidence exists in support of a theoretical relationship between Q and food ingestion. The conclusion follows that some knowledge of the protein limit mass (α) and of the point of inflection (related to X + Z) is the main requirement for the application of the theory for description and prediction in animal nutrition and breeding. protein growth curves intake prediction animal improvement Animal culture In Animal Elsevier, 2021 5(2011), 3, Seite 439-449 (DE-627)534060382 (DE-600)2365209-3 1751732X nnns volume:5 year:2011 number:3 pages:439-449 https://doi.org/10.1017/S1751731110001874 kostenfrei https://doaj.org/article/7b6bdf01ddb640cb813905b2f448d0b1 kostenfrei http://www.sciencedirect.com/science/article/pii/S1751731110001874 kostenfrei https://doaj.org/toc/1751-7311 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_90 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_151 GBV_ILN_161 GBV_ILN_165 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 5 2011 3 439-449 |
spelling |
10.1017/S1751731110001874 doi (DE-627)DOAJ05654281X (DE-599)DOAJ7b6bdf01ddb640cb813905b2f448d0b1 DE-627 ger DE-627 rakwb eng SF1-1100 C.Z. Roux verfasserin aut A family of protein growth curves with extension to other chemical body components together with application to animal nutrition and improvement 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Theory that successfully explains the magnitude and range of estimates of protein retention (PR) efficiency from the cost of turnover of existing protein indicates that conventional curves for growth description are inappropriate for protein growth. A solution to this problem is found in the consideration that the rate-limiting steps for protein synthesis (PS) and breakdown are likely to be associated with the diffusion of metabolites in and between cells. The algebraic scaling of nuclear and cellular diffusion capacity with tissue or total body protein leads to a parameterization of the primal differential equation for PR (kg/day) based on two terms representing PS and breakdown, viz. PR = cQ[(P/α)X + Z - (4/9)Y — (P/α)X + Z]. where c is an arbitrary constant, Q is the proportion of nuclei active in cell growth or division in a tissue or the whole body, α is the limit mass for protein (P, kg) in a tissue or the whole body, the power X + Z represents the rate-limiting steps in protein breakdown and Y is the power of the relationship between cell volume and the amount of tissue protein. For the whole body, the contribution of the different tissues should be weighted in proportion to their PS rates with, on average, Y = 1/2. The constant 4/9 arises from the scaling of the specific diffusion rate of DNA activator precursors from nuclear dimensions and from the relationship between nuclear and cell volume. Experimental evidence on protein breakdown rate as well as protein and body mass points of inflection indicates that the range of theoretically possible numerical values of the rate-limiting powers X + Z = (i + 3)/9 for i = 1, 2, …,12 seems adequate for the description of the range of observed whole body protein and body mass growth patterns for mammals. Q = 1 represents maximal protein retention, and for 0 < Q < 1, experimental evidence exists in support of a theoretical relationship between Q and food ingestion. The conclusion follows that some knowledge of the protein limit mass (α) and of the point of inflection (related to X + Z) is the main requirement for the application of the theory for description and prediction in animal nutrition and breeding. protein growth curves intake prediction animal improvement Animal culture In Animal Elsevier, 2021 5(2011), 3, Seite 439-449 (DE-627)534060382 (DE-600)2365209-3 1751732X nnns volume:5 year:2011 number:3 pages:439-449 https://doi.org/10.1017/S1751731110001874 kostenfrei https://doaj.org/article/7b6bdf01ddb640cb813905b2f448d0b1 kostenfrei http://www.sciencedirect.com/science/article/pii/S1751731110001874 kostenfrei https://doaj.org/toc/1751-7311 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_90 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_151 GBV_ILN_161 GBV_ILN_165 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 5 2011 3 439-449 |
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10.1017/S1751731110001874 doi (DE-627)DOAJ05654281X (DE-599)DOAJ7b6bdf01ddb640cb813905b2f448d0b1 DE-627 ger DE-627 rakwb eng SF1-1100 C.Z. Roux verfasserin aut A family of protein growth curves with extension to other chemical body components together with application to animal nutrition and improvement 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Theory that successfully explains the magnitude and range of estimates of protein retention (PR) efficiency from the cost of turnover of existing protein indicates that conventional curves for growth description are inappropriate for protein growth. A solution to this problem is found in the consideration that the rate-limiting steps for protein synthesis (PS) and breakdown are likely to be associated with the diffusion of metabolites in and between cells. The algebraic scaling of nuclear and cellular diffusion capacity with tissue or total body protein leads to a parameterization of the primal differential equation for PR (kg/day) based on two terms representing PS and breakdown, viz. PR = cQ[(P/α)X + Z - (4/9)Y — (P/α)X + Z]. where c is an arbitrary constant, Q is the proportion of nuclei active in cell growth or division in a tissue or the whole body, α is the limit mass for protein (P, kg) in a tissue or the whole body, the power X + Z represents the rate-limiting steps in protein breakdown and Y is the power of the relationship between cell volume and the amount of tissue protein. For the whole body, the contribution of the different tissues should be weighted in proportion to their PS rates with, on average, Y = 1/2. The constant 4/9 arises from the scaling of the specific diffusion rate of DNA activator precursors from nuclear dimensions and from the relationship between nuclear and cell volume. Experimental evidence on protein breakdown rate as well as protein and body mass points of inflection indicates that the range of theoretically possible numerical values of the rate-limiting powers X + Z = (i + 3)/9 for i = 1, 2, …,12 seems adequate for the description of the range of observed whole body protein and body mass growth patterns for mammals. Q = 1 represents maximal protein retention, and for 0 < Q < 1, experimental evidence exists in support of a theoretical relationship between Q and food ingestion. The conclusion follows that some knowledge of the protein limit mass (α) and of the point of inflection (related to X + Z) is the main requirement for the application of the theory for description and prediction in animal nutrition and breeding. protein growth curves intake prediction animal improvement Animal culture In Animal Elsevier, 2021 5(2011), 3, Seite 439-449 (DE-627)534060382 (DE-600)2365209-3 1751732X nnns volume:5 year:2011 number:3 pages:439-449 https://doi.org/10.1017/S1751731110001874 kostenfrei https://doaj.org/article/7b6bdf01ddb640cb813905b2f448d0b1 kostenfrei http://www.sciencedirect.com/science/article/pii/S1751731110001874 kostenfrei https://doaj.org/toc/1751-7311 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_90 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_151 GBV_ILN_161 GBV_ILN_165 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 5 2011 3 439-449 |
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10.1017/S1751731110001874 doi (DE-627)DOAJ05654281X (DE-599)DOAJ7b6bdf01ddb640cb813905b2f448d0b1 DE-627 ger DE-627 rakwb eng SF1-1100 C.Z. Roux verfasserin aut A family of protein growth curves with extension to other chemical body components together with application to animal nutrition and improvement 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Theory that successfully explains the magnitude and range of estimates of protein retention (PR) efficiency from the cost of turnover of existing protein indicates that conventional curves for growth description are inappropriate for protein growth. A solution to this problem is found in the consideration that the rate-limiting steps for protein synthesis (PS) and breakdown are likely to be associated with the diffusion of metabolites in and between cells. The algebraic scaling of nuclear and cellular diffusion capacity with tissue or total body protein leads to a parameterization of the primal differential equation for PR (kg/day) based on two terms representing PS and breakdown, viz. PR = cQ[(P/α)X + Z - (4/9)Y — (P/α)X + Z]. where c is an arbitrary constant, Q is the proportion of nuclei active in cell growth or division in a tissue or the whole body, α is the limit mass for protein (P, kg) in a tissue or the whole body, the power X + Z represents the rate-limiting steps in protein breakdown and Y is the power of the relationship between cell volume and the amount of tissue protein. For the whole body, the contribution of the different tissues should be weighted in proportion to their PS rates with, on average, Y = 1/2. The constant 4/9 arises from the scaling of the specific diffusion rate of DNA activator precursors from nuclear dimensions and from the relationship between nuclear and cell volume. Experimental evidence on protein breakdown rate as well as protein and body mass points of inflection indicates that the range of theoretically possible numerical values of the rate-limiting powers X + Z = (i + 3)/9 for i = 1, 2, …,12 seems adequate for the description of the range of observed whole body protein and body mass growth patterns for mammals. Q = 1 represents maximal protein retention, and for 0 < Q < 1, experimental evidence exists in support of a theoretical relationship between Q and food ingestion. The conclusion follows that some knowledge of the protein limit mass (α) and of the point of inflection (related to X + Z) is the main requirement for the application of the theory for description and prediction in animal nutrition and breeding. protein growth curves intake prediction animal improvement Animal culture In Animal Elsevier, 2021 5(2011), 3, Seite 439-449 (DE-627)534060382 (DE-600)2365209-3 1751732X nnns volume:5 year:2011 number:3 pages:439-449 https://doi.org/10.1017/S1751731110001874 kostenfrei https://doaj.org/article/7b6bdf01ddb640cb813905b2f448d0b1 kostenfrei http://www.sciencedirect.com/science/article/pii/S1751731110001874 kostenfrei https://doaj.org/toc/1751-7311 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_90 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_151 GBV_ILN_161 GBV_ILN_165 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 5 2011 3 439-449 |
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family of protein growth curves with extension to other chemical body components together with application to animal nutrition and improvement |
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A family of protein growth curves with extension to other chemical body components together with application to animal nutrition and improvement |
abstract |
Theory that successfully explains the magnitude and range of estimates of protein retention (PR) efficiency from the cost of turnover of existing protein indicates that conventional curves for growth description are inappropriate for protein growth. A solution to this problem is found in the consideration that the rate-limiting steps for protein synthesis (PS) and breakdown are likely to be associated with the diffusion of metabolites in and between cells. The algebraic scaling of nuclear and cellular diffusion capacity with tissue or total body protein leads to a parameterization of the primal differential equation for PR (kg/day) based on two terms representing PS and breakdown, viz. PR = cQ[(P/α)X + Z - (4/9)Y — (P/α)X + Z]. where c is an arbitrary constant, Q is the proportion of nuclei active in cell growth or division in a tissue or the whole body, α is the limit mass for protein (P, kg) in a tissue or the whole body, the power X + Z represents the rate-limiting steps in protein breakdown and Y is the power of the relationship between cell volume and the amount of tissue protein. For the whole body, the contribution of the different tissues should be weighted in proportion to their PS rates with, on average, Y = 1/2. The constant 4/9 arises from the scaling of the specific diffusion rate of DNA activator precursors from nuclear dimensions and from the relationship between nuclear and cell volume. Experimental evidence on protein breakdown rate as well as protein and body mass points of inflection indicates that the range of theoretically possible numerical values of the rate-limiting powers X + Z = (i + 3)/9 for i = 1, 2, …,12 seems adequate for the description of the range of observed whole body protein and body mass growth patterns for mammals. Q = 1 represents maximal protein retention, and for 0 < Q < 1, experimental evidence exists in support of a theoretical relationship between Q and food ingestion. The conclusion follows that some knowledge of the protein limit mass (α) and of the point of inflection (related to X + Z) is the main requirement for the application of the theory for description and prediction in animal nutrition and breeding. |
abstractGer |
Theory that successfully explains the magnitude and range of estimates of protein retention (PR) efficiency from the cost of turnover of existing protein indicates that conventional curves for growth description are inappropriate for protein growth. A solution to this problem is found in the consideration that the rate-limiting steps for protein synthesis (PS) and breakdown are likely to be associated with the diffusion of metabolites in and between cells. The algebraic scaling of nuclear and cellular diffusion capacity with tissue or total body protein leads to a parameterization of the primal differential equation for PR (kg/day) based on two terms representing PS and breakdown, viz. PR = cQ[(P/α)X + Z - (4/9)Y — (P/α)X + Z]. where c is an arbitrary constant, Q is the proportion of nuclei active in cell growth or division in a tissue or the whole body, α is the limit mass for protein (P, kg) in a tissue or the whole body, the power X + Z represents the rate-limiting steps in protein breakdown and Y is the power of the relationship between cell volume and the amount of tissue protein. For the whole body, the contribution of the different tissues should be weighted in proportion to their PS rates with, on average, Y = 1/2. The constant 4/9 arises from the scaling of the specific diffusion rate of DNA activator precursors from nuclear dimensions and from the relationship between nuclear and cell volume. Experimental evidence on protein breakdown rate as well as protein and body mass points of inflection indicates that the range of theoretically possible numerical values of the rate-limiting powers X + Z = (i + 3)/9 for i = 1, 2, …,12 seems adequate for the description of the range of observed whole body protein and body mass growth patterns for mammals. Q = 1 represents maximal protein retention, and for 0 < Q < 1, experimental evidence exists in support of a theoretical relationship between Q and food ingestion. The conclusion follows that some knowledge of the protein limit mass (α) and of the point of inflection (related to X + Z) is the main requirement for the application of the theory for description and prediction in animal nutrition and breeding. |
abstract_unstemmed |
Theory that successfully explains the magnitude and range of estimates of protein retention (PR) efficiency from the cost of turnover of existing protein indicates that conventional curves for growth description are inappropriate for protein growth. A solution to this problem is found in the consideration that the rate-limiting steps for protein synthesis (PS) and breakdown are likely to be associated with the diffusion of metabolites in and between cells. The algebraic scaling of nuclear and cellular diffusion capacity with tissue or total body protein leads to a parameterization of the primal differential equation for PR (kg/day) based on two terms representing PS and breakdown, viz. PR = cQ[(P/α)X + Z - (4/9)Y — (P/α)X + Z]. where c is an arbitrary constant, Q is the proportion of nuclei active in cell growth or division in a tissue or the whole body, α is the limit mass for protein (P, kg) in a tissue or the whole body, the power X + Z represents the rate-limiting steps in protein breakdown and Y is the power of the relationship between cell volume and the amount of tissue protein. For the whole body, the contribution of the different tissues should be weighted in proportion to their PS rates with, on average, Y = 1/2. The constant 4/9 arises from the scaling of the specific diffusion rate of DNA activator precursors from nuclear dimensions and from the relationship between nuclear and cell volume. Experimental evidence on protein breakdown rate as well as protein and body mass points of inflection indicates that the range of theoretically possible numerical values of the rate-limiting powers X + Z = (i + 3)/9 for i = 1, 2, …,12 seems adequate for the description of the range of observed whole body protein and body mass growth patterns for mammals. Q = 1 represents maximal protein retention, and for 0 < Q < 1, experimental evidence exists in support of a theoretical relationship between Q and food ingestion. The conclusion follows that some knowledge of the protein limit mass (α) and of the point of inflection (related to X + Z) is the main requirement for the application of the theory for description and prediction in animal nutrition and breeding. |
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A family of protein growth curves with extension to other chemical body components together with application to animal nutrition and improvement |
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