Functional differentiation in embryonic development: I. Cholinesterase activity of induced neural structures in Amblystoma punctatum

Boell, E. J.; Shen, Shih‐Chang

doi:10.1002/jez.1400970103

Cited by 37 publications

(4 citation statements)

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“…This ultramicro manometric method, extensively investigated by LINDER-STR0M-LANG, HoLTER, and ZEUTHEN, was applied for the first time by LINDER-STR0M-LANG and GLICK (1938) to the assay of serum ChE and later by BoELL and SHEN (1944) in their study of ChE in developing Amblystoma. The method was improved considerably by ZAJICEK and ZEUTHEN (1956) for ChE determinations with single cells (e.g., nerve cells, megakaryocytes) and later used by GIA-COBINI (1959) in his studies on isolated ganglion cells and even their constituent organelles (i.e., nucleus, nucleolus).…”

Section: Cartesian Diver Techniquementioning

confidence: 99%

Classification and Comparative Enzymology of the Cholinesterases and Methods for their Determination

Augustinsson¹

1963

Cholinesterases and Anticholinesterase Agents

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Section: Cartesian Diver Techniquementioning

confidence: 99%

Classification and Comparative Enzymology of the Cholinesterases and Methods for their Determination

Augustinsson¹

1963

Cholinesterases and Anticholinesterase Agents

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“…Unlike vertebrate brain which contains only specific cholinesterase activity (185), the peripheral nerves of the rat and the dog contain both enzymes (188). The differentiation of the ne r vous system in the developing embryo of the spotted salamander was found to be accompanied by an increase in the concentration of cholinesterase in the nervous tissues ; more over, neural structures secondarily induced by experimentally im planted tissue resembled primary nervous tissue with respect to cho linesterase activity (189) . The cholinesterase of human and dog erythrocytes is said to be attached to the stroma of the cells (190).…”

Section: Non-proteolytic Enzymesmentioning

confidence: 97%

Non-Oxidative Enzymes

1946

Annu. Rev. Biochem.

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An extensive account of recent work on enzymes which hydrolyze the peptide linkage was given by Greenberg & Winnick in last year's Annual Review of Biochemistry (1). The present discussion of these enzymes is necessarily limited to a consideration of a relatively small number of contributions selected from the more recent literature.Plant proteinases.-To the list of these enzymes previously re corded (1) may now be added the pro teinase "arachain" which was isolated in purified form from the cotyledons and embryo of the pea nut by Irving & Fontaine (2). This enzyme functions optimally at pH 6.5 to 7. 5 and its activity is not influenced by cyanide, cysteine, or hydrogen peroxide. when these compounds are present in concen trations which have a marked effect on several other proteinases. Moreover, the hydrolysis of the synthetic substrate benzoyl-I-arginine amide was shown to proceed in the first stages as a reaction of zero order, even at very low concentrations of substrate. The authors point out that this behavior differs from that of other proteolytic en zymes whose reaction kinetics have been studied. In practically all other cases the kinetics of the hydrolysis of synthetic substrates are those of first order reactions. Castaneda and co-workers (3) have succeeded in crystallizing the enzyme mexicain which is found in the latex of Pileus me.ricanus.Digestion of native and denatured proteins.-The fact that de natured proteins are, in many instances, more readily hydrolyzed by enzymes than the corresponding native proteins seems now to be well established. In a comparative study of the papain-digestion of native human serum albumin and of this protein after denaturation by heat and by urea, Rice and co-workers (4) have observed some interest ing effects of sodium caprylate and of the sodium sal�s of other acids such as phenyl butyric acid on the denaturation pro' cess. Each of these salts not only protects native serum albumin from undergoing coagulation at a temperature at which the protein is quickly coagulated in the absence of the salt; but the salts also have the effect of "stabiliz ing" the protein during treatment by urea or by heat in such a man-35 Annu. Rev. Biochem. 1946.15:35-74. Downloaded from www.annualreviews.org Access provided by Northeastern University on 02/02/15. For personal use only. Quick links to online content Further ANNUAL REVIEWS

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“…Nervous system.-An investigation of chemical changes which may take place in induced neural structures has been undertaken by Boell & Shen (36). They have found that the cholinesterase activity of secondary, induced neural structures in Amblystoma punctatum is of the same order as that of the primary neural tissues of the host and much greater than that of ectoderm which did not receive the stimulus of induction.…”

mentioning

confidence: 99%

Developmental Physiology

Flexner¹

1946

Annu. Rev. Physiol.

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voted to a presentation of the recent additions to our understand ing of the development of the mammalian embryo and fetus. The fie�d is one of exceptional breadth and considerable activity for it has stimulated interest in many branches of animal biology. Con tributing to it are the classical embryologist and anatomist inter ested primarily in problems of morphogenesis; the physiologist and zoologist investigating the development of function; the biochem ist concerned with chemical differentiation and the chemical dif ferences which exist between typical and atypical cellular growth; the obstetrician and pediatrician who add a clinical interest to problems of fetal nutrition and of fetal anomalies. It will be ap parent that these various points of view are interdependent and that a presentation of progress in developmental physiology must include the advances made in its closely related fields of interest.

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Functional differentiation in embryonic development: I. Cholinesterase activity of induced neural structures in Amblystoma punctatum

Cited by 37 publications

References 20 publications

Classification and Comparative Enzymology of the Cholinesterases and Methods for their Determination

Classification and Comparative Enzymology of the Cholinesterases and Methods for their Determination

Non-Oxidative Enzymes

Developmental Physiology

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