Determination of Aldolase in Animal Tissues

Sibley, John A.; Lehninger, Albert L.

doi:10.1016/s0021-9258(18)57031-9

Cited by 523 publications

(13 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The presence of a highly active epimerase in extracts from muscle and tumour cells, and its almost complete absence from erythrocytes, is further evidence of the separate nature of PPI and epimerase. This distribution is similar to that of aldolase, in which the erythrocytes are exceptionally weak (Sibley & Lehninger, 1949; see also Table 4): it is interesting to note the tightly bound association of epimerase with aldolase, which persists on recrystallization, reported by Horecker et al (1956).…”

Section: Discussionsupporting

confidence: 73%

See 1 more Smart Citation

Pentose phosphate isomerase and epimerase from animal tissues

Dickens

Williamson

1956

Biochemical Journal

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 73%

“…Aldolase activity compared with pentose phosphate-isomerase activity of extracts Period of incubation: for aldolase, 15 min. at 300 with fructose 1:6-diphosphate (FDP) in 01M tris buffer, pH 8-6 (method ofSibley & Lehninger, 1949). For PPI, usual assay conditions (see Methods); 10 min.…”

mentioning

confidence: 99%

Pentose phosphate isomerase and epimerase from animal tissues

Dickens

Williamson

1956

Biochemical Journal

View full text Add to dashboard Cite

“…The enzyme was stored as a suspension in the crystallizing medium at 2°until used. Such preparations had specific activities of 49-56 units/mg when assayed by the method of Sibley and Lehninger (1949) as modified by Swenson and Boyer (1957).…”

Section: Methodsmentioning

confidence: 99%

The Dissociation and Reconstitution of Aldolase^*

Stellwagen¹,

Schachman²

1962

Biochemistry

208

View full text Add to dashboard Cite

Rabbit muscle aldolase, which exists in solution as essentially globular, compact, highly organized particles of molecular weight 1.42 X 106, was readily dissociated into three polypeptide chains apparently without the rupture of covalent bonds. This dissociation was effected by treatment with any of the reagents, urea, HC1, acetic acid, or sodium dodecyl sulfate. Detailed studies of the subunits generated in 4 m urea solutions at pH 5.5 and in acid solutions (pH 2) showed that the polypeptide chains were markedly disorganized as coil-like particles of weight-average molecular weight 0.46 X 105. Upon dissociation and denaturation the reduced viscosity increased from 4.0 ml/g for the native enzyme to 23 ml/g at pH 2 and 18 ml/g in 4 m urea solutions. The optical rotation, [a]d, changed from -23°for the native protein to -62°and -83°for the aciddissociated and urea-dissociated subunits respectively. Similarly there was a marked change in the Drude constant, Ac, from 283 mp to 238 mp and 223 m^i. Accompanying the change in the conformation of the polypeptide chains was a blue shift in the absorption spectrum with AmaI decreasing from 279.7 mp for the native protein to 277.0 mp for the subunits. Analyses of the shift by difference spectra revealed contributions from chromophoric groups of tyrosine, tryptophan, and phenylalanine due to the altered environment of these chromophores in the dissociated chains as compared to the intact enzyme. Titration of the sulfhydryl groups showed that the 16 groups which are "masked" in the native enzyme reacted readily in the dissociated subunits.No enzymic activity could be detected in the subunits in the presence of urea. However, activity was regained with yields of 65% when the dissociating agents (hydrogen ions or urea) were removed by dilution or dialysis. Reconstitution experiments were performed under different conditions; pH 5.5 and concentrations greater than about 50 /il/ml were found to be optimal for the restoration of activity. Kinetic studies showed that extensive annealing was unnecessary, for enzymic activity was regained in only a few minutes. The reconstituted protein was characterized by its reduced viscosity, sedimentation coefficient, molecular weight, optical rotatory dispersion, absorption spectrum, titratable sulfhydryl groups, and specific activity. In all respects the reconstituted macromolecules were virtually identical to the native enzyme.

show abstract

“…An activity of pFBA in pooled leaves was measured according to the modified method of Sibley-Lehninger [65,66]. Chloroplast proteins were extracted as described by Kosmala et al (2012) and Perlikowski et al (2016) with slight modifications [5,8].…”

Section: Activity Of Chloroplast Aldolasementioning

confidence: 99%

Two Festuca Species—F. arundinacea and F. glaucescens—Differ in the Molecular Response to Drought, While Their Physiological Response Is Similar

Lechowicz

Pawłowicz

Perlikowski

et al. 2020

IJMS

View full text Add to dashboard Cite

Impact of photosynthetic and antioxidant capacities on drought tolerance of two closely related forage grasses, Festuca arundinacea and Festuca glaucescens, was deciphered. Within each species, two genotypes distinct in drought tolerance were subjected to a short-term drought, followed by a subsequent re-watering. The studies were focused on: (i) analysis of plant physiological performance, including: water uptake, abscisic acid (ABA) content, membrane integrity, gas exchange, and relative water content in leaf tissue; (ii) analysis of plant photosynthetic capacity (chlorophyll fluorescence; gene expression, protein accumulation, and activity of selected enzymes of the Calvin cycle); and (iii) analysis of plant antioxidant capacity (reactive oxygen species (ROS) generation; gene expression, protein accumulation and activity of selected enzymes). Though, F. arundinacea and F. glaucescens revealed different strategies in water uptake, and partially also in ABA signaling, their physiological reactions to drought and further re-watering, were similar. On the other hand, performance of the Calvin cycle and antioxidant system differed between the analyzed species under drought and re-watering periods. A stable efficiency of the Calvin cycle in F. arundinacea was crucial to maintain a balanced network of ROS/redox signaling, and consequently drought tolerance. The antioxidant capacity influenced mostly tolerance to stress in F. glaucescens.

show abstract

Determination of Aldolase in Animal Tissues

Cited by 523 publications

References 9 publications

Pentose phosphate isomerase and epimerase from animal tissues

Pentose phosphate isomerase and epimerase from animal tissues

The Dissociation and Reconstitution of Aldolase^*

Two Festuca Species—F. arundinacea and F. glaucescens—Differ in the Molecular Response to Drought, While Their Physiological Response Is Similar

Contact Info

Product

Resources

About

Determination of Aldolase in Animal Tissues

Cited by 523 publications

References 9 publications

Pentose phosphate isomerase and epimerase from animal tissues

Pentose phosphate isomerase and epimerase from animal tissues

The Dissociation and Reconstitution of Aldolase*

Two Festuca Species—F. arundinacea and F. glaucescens—Differ in the Molecular Response to Drought, While Their Physiological Response Is Similar

Contact Info

Product

Resources

About

The Dissociation and Reconstitution of Aldolase^*