Intracellular localization of glycolytic enzymes in cross-striated muscles of locusta migratoria

Pette, Dirk; Brandau, H.

doi:10.1016/0006-291x(62)90056-6

Cited by 57 publications

(7 citation statements)

References 6 publications

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“…In our studies on changes in the metabolism of neoplastic and insulted cells in tissues, the activities of several key enzymes are assayed in situ with the agarose gel film technique originally introduced by Pette and his colleagues (Pette & Brandau, 1962;Nolte & Pette, 1971, 1972aPette & Wimmer, 1979). This technique is technically simpler to use than tissue stabilizer and other methods for sequential assays of several enzymes in the same section.…”

Section: Introductionmentioning

confidence: 99%

Estimating the initial reaction velocity of a soluble dehydrogenase in situ

Nakae

Stoward

1993

Histochem J

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The initial reaction velocities (vi) of lactate dehydrogenase in single hepatocytes were determined, by microdensitometry or computer-assisted image analysis, in sections of unfixed mouse liver incubated at 37 degrees C on substrate-containing agarose gel films. They were found to fit the equations vi = 2.82 degrees A and vi = vi + 2 degrees A, where vi and degrees A are, respectively, the gradients (or steady-state linear velocities) and the intercepts on the absorbance axis of the linear regression lines of the absorbance (A) on incubation time plots for incubation times between 1 and 3 min. Both equations were independent of section thickness between 4 and 14 microns. The observed and calculated values of vi agreed within 11.5% (n = 71). The validity of the equations for vi was confirmed by showing that the calculated vi was proportional to the thickness of the section and hence the amount of enzyme present. Thus, vi can be determined from measurements of either degrees A alone or vi and degrees A.

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Section: Introductionmentioning

confidence: 99%

Estimating the initial reaction velocity of a soluble dehydrogenase in situ

Nakae

Stoward

1993

Histochem J

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“…Besides binding to purified actin, aldolase A4 also binds less firmly to other protein fractions from muscle, including actomyosin, myosin and 'stroma protein' {Arnold and Pette, 1968). Pette and Brandau (1962) have observed histochem ical staining patterns similar to the one shown in figure 2 for several other muscle enzymes, including phosphorylase, glyceraldehyde-3-phosphate dehy drogenase and lactate dehydrogenase. These enzymes all increase in specific activity during muscle development, although not strictly parallel with changes in CPK, aldolase and myosin (Hauschka, 1968).…”

Section: And For Mm-cpk (Yagi and Mase 1962) Mm-cpk Does Not Bind Tmentioning

confidence: 88%

Developmental Changes in Creatine Kinase and Aldolase Isoenzymes and their Possible Function in Association with Contractile Elements

Turner¹,

Eppenberger²

1973

Enzyme Protein

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Tissue specific isoenzyme distributions of creatine kinase and aldolase in muscle and brain of chicken and rat show similarities suggesting coordinate regulation of these two enzymes. In vitro studies of chick skeletal muscle differentiation provide evidence for parallel changes in the activities and isoenzyme patterns of creatine kinase and aldolase occurring concomitantly with increased myosin synthesis following myoblast fusion. It has recently been demonstrated that one of the homodimers of creatine kinase binds specifically to the M-line of the skeletal muscle myofibril. There is evidence that aldolase A(4) also binds to the myofibril, at the I-band. The possibility that these and other myofibrillar proteins might be coordinately regulated in muscle development is discussed. Furthermore, on the basis of correlations with tissue distributions of myofibrillar and non-myofibrillar actomyosin, it is proposed that levels of creatine kinase isoenzymes may be regulated in different tissues according to the type of actomyosin present.

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“…Although we have studied the problem of adsorption in some detail (Hultin et al, 1966b), no clear-cut conclusions can be drawn on the basis of our results to date as to whether the LDH is associated with the subcellular structure in situ or is adsorbed during homogenization of the muscle. Several reports utilizing cytochemical techniques (Pette et al, 1962 ;Van-Wijhe et al, 1964 ;Fahimi et al, 1964) have indicated a particulate site for LDH in striated muscle. Amberson et al (1965)) using a different approach, have concluded that at least part of the LDH in rabbit muscle is attached to the ultrastructure.…”

Section: The Sarcolemmamentioning

confidence: 98%

Sarcolemmae from Chicken Skeletal Muscle. 2. Properties

Hultin

Westort

1969

Journal of Food Science

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SUMMARY– Sarcolemmae are usually identified solely by morphological characteristics. We have determined several chemical and enzymic properties of sarcolemmae from chicken breast muscle prepared by homogenization of aged muscle in dilute CaCl2 solution, washing 4 times in NaCl‐histidine at pH 7.4, extraction with water buffered to pH 7 and isolation by differential centrifugation on a discontinuous sucrose gradient. The phospholipid content of the sarcolemmae was low, representing only 2 to 3% by weight compared with the 20 to 35% usually found in membraneous systems. This discrepancy may be due to the relatively small proportion of plasma membrane in the sarcolemma.Analyses indicate little contamination by nuclei or mitochondria. The sarcolemmae have, like the microsomal fraction, high contents of RNA and glucose‐6‐phosphatase activity. The sarcolemma is either rich in these elements or is contaminated by other subcellular elements, such as the transverse tubules (T system), which are. The sarcolemmae display a Mg+2‐ activated ATPase activity which is typical for membraneous systems. Lactate dehydrogenase was shown to be associated with the sarcolemmae. Whether this represents the situation in vivo or is an artifact of preparation is not clear. The sarcolemmae are capable of binding soluble LDH.

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Intracellular localization of glycolytic enzymes in cross-striated muscles of locusta migratoria

Cited by 57 publications

References 6 publications

Estimating the initial reaction velocity of a soluble dehydrogenase in situ

Estimating the initial reaction velocity of a soluble dehydrogenase in situ

Developmental Changes in Creatine Kinase and Aldolase Isoenzymes and their Possible Function in Association with Contractile Elements

Sarcolemmae from Chicken Skeletal Muscle. 2. Properties

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