La croissance de la C. G. T.

Kriegel, Annie

doi:10.1515/9783111395913

Cited by 7 publications

(3 citation statements)

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“…Solution measurements indicate the native octameric enzyme has a sedimentation coefficient of 21 S and a molecular mass of about 800 kDa (Kopperschlager et al, 1977;Chaffotte et al, 1984). The octameric structure of the native enzyme is stable at a protein concentration of 1 mg/ ml at ambient temperature and neutral pH in the presence or absence of substrates or allosteric effectors (Kriegel et al, 1986(Kriegel et al, , 1987.…”

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Limited proteolysis of yeast phosphofructokinase

Kopperschläger

Bär

Stellwagen

1993

European Journal of Biochemistry

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Purified phosphofructokinase 1 from baker's yeast (Saccharomyces cerevisiae) was subjected to proteol ysis by thermolysin, endoproteinase lys-C, trypsin and chymotrypsin under defined solvent conditions. In the absence of substrates and allosteric effectors, the catalytic activity of phosphofructokinase rapidly disappeared in the presence of each proteolytic enzyme. The presence of a saturating concentration of ATP protected phosphofructokinase activity from proteolytic inactivation while the collective presence of fructose 6-phosphate, AMP and fructose 2,6-bisphosphate provided transient activation during proteolysis.Changes in the quaternary structure of phosphofructokinase resulting from proteolysis were estimated by high performance size exclusion chromatography while changes in the primary sequence of the individual a and p polypeptide chains were estimated by polyacrylamide-gel electrophoresis in sodium dodecylsulfate. The site(s) of proteolytic cleavage were identified by N-terminal sequence analysis of resolved electrophoretic components.The presence of ATP protects phosphofructokinase from thermolysin proteolysis, while the collective presence of fructose 6-phosphate, AMP and fructose 2,6-bisphosphate restricts proteolysis to one site in each polypeptide chain involving the peptide bonds preceding Leu199 in the a chain and Leu192 in the p chain. The truncated phosphofructokinase retains its octameric structure. The presence of ATP largely restricts endoproteinase lys-C proteolysis to a single site in the n chain involving the peptide bond preceding Va1914. This cleavage results in the dissociation of the octameric form of phosphofructokinase into two tetramers. The presence of ATP restricts both trypsin and chymotrypsin proteolysis to the N-terminal and C-terminal regions described above, resulting in the preferential stabilization of the tetrameric form of phosphofructokinase.It would appear that the first 200 and last 80 residues which are unique to the sequence of the yeast phosphosphofructokinase are not directly involved in catalysis or its allosteric regulation.However, the last 80 residues of the a polypeptide chain do appear to stabilize an octameric structure which is unique to yeast phosphofructokinase.Yeast phosphofructokinase 1 contains two kinds of polypeptide chains, an a chain containing 987 residues in a known sequence and encoded by the PFKl gene and a chain containing 959 residues, also in a known sequence encoded by the PFK2 gene (Heinisch et a]., 1989). The native enzyme is a globular protein containing four a chains and four p chains. Solution measurements indicate the native octameric enzyme has a sedimentation coefficient of 21 S and a molecular mass of about 800 kDa (Kopperschlager et al., 1977;Chaffotte et al., 1984). The octameric structure of the native enzyme is stable at a protein concentration of 1 mg/ ml at ambient temperature and neutral pH in the presence or Correspondence to

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“…Phoaphofructokinase (EC 2.7.1.11); trypsiu (EC 3.4.21.4); chymotrypsin (EC 3.4.21.1); thermolysin (EC 3.4.24.4); lys-C (EC 3.4.21 SO); aldolase (EC 4.1.2.13); glycerophosphate dehydrogenase (EC 1 .I .1.8); triosephosphate isomerase (EC 5.3.1.1). absence of substrates or allosteric effectors (Kriegel et al, 1986(Kriegel et al, , 1987.…”

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confidence: 99%

Limited proteolysis of yeast phosphofructokinase

Kopperschläger

Bär

Stellwagen

1993

European Journal of Biochemistry

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“…(2010) for recent technological adoption in the US dairy sector. Discussions on the improvement of rotational grazing are found in Kriegel and Frank (2005); Taylor and Foltz (2006); Winsten et al (2010); Nelson et al (2014).…”

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Dairy Productivity and Technical Change: An Analysis of Confinement and Management Intensive Grazing Dairies in Maryland for 1995–2009

Minegishi

Johnson

2017

Agric. Resour. Econom. Rev.

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.S. dairy production has been consolidating into large-scale confinement operations. Large numbers of small-to medium-scale dairies have disappeared in the last two decades, and many more are disappearing. This article analyzes small-to medium-scale dairy operations in Maryland during 1995-2009 for changes in technology and efficiency through a novel two-stage DEA approach to examine productivity changes. Conventional confinement dairy operations and management-intensive grazing dairies are analyzed separately. The results show that both dairy systems have become more productive on the technological frontiers, yet the rate of technical change for graziers was less than half the rate for confinement.

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Industrial Relations Research in France 1960–75: A Review

Reynaud¹

1981

Industrial Relations in International Perspective

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La croissance de la C. G. T.

Cited by 7 publications

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Limited proteolysis of yeast phosphofructokinase

Limited proteolysis of yeast phosphofructokinase

Dairy Productivity and Technical Change: An Analysis of Confinement and Management Intensive Grazing Dairies in Maryland for 1995–2009

Industrial Relations Research in France 1960–75: A Review

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