EXTRACELLULAR ENZYMES FROM STRAINS OF SORANGIUM

1965 ◽  
Vol 11 (1) ◽  
pp. 109-118 ◽  
Author(s):  
D. C. Gillespie ◽  
F. D. Cook

Soil organisms belonging to the myxobacter group and predatory on molds, yeasts, nematodes, and streptomycetes as well as on a wide range of bacteria elaborate at least two extracellular enzymes: a protease and a lysin. The protease hydrolyzes casein and haemoglobin and is inactive against bacterial cell walls while the lysin hydrolyzes bacterial cell walls but is inactive on proteins. These enzymes have been separated on hydroxylapatite columns and some of their properties are described. The predatory action of many of the isolates may be explained by the secretion and subsequent action of these two enzymes.

1968 ◽  
Vol 170 (1021) ◽  
pp. 331-348 ◽  

A glance at previous Leeuwenhoek Lectures reveals that in a number of cases the Lecturer has felt obliged to preface his account with an apology to the effect that the subject of his lecture would seem to bear little relationship to the distinguished work of Antony van Leeuwenhoek. In my case, however, such apology is unnecessary as a reasonably direct connexion can be established between those remarkable observations in the seventeenth century and the work described here. Leeuwenhoek’s description of bacteria is based on their appearance under his primitive but remarkably effective microscopes. Such appearance is, of course, governed by shape and we see from the published record that cocci, bacilli and spirochaetes were observed and accurately described in terms of size and shape. These features are functions of the nature and rigidity of the wall surrounding the organisms and so are related to molecular structure; the purpose of my lecture is to describe certain aspects of the recently acquired knowledge of the molecular architecture of bacterial cell walls. The great interest that has developed in the chemistry and biochemistry of bacterial cell walls during the last ten years or so has arisen for a number of reasons (cf. Salton 1964). In the first place, walls are of interest because they represent a substantial proportion of the metabolic products of the cell; they frequently comprise up to 20% of the dry weight of cells and so must be regarded as important metabolites. Moreover, their chemical structure is interesting in view of their physical properties. Thus, besides being reasonably rigid structures with considerable strength they are nevertheless freely permeable towards cellular products and nutrients. Under certain conditions even large molecules such as antibodies, extracellular enzymes and nucleic acids can penetrate the wall, although the full extent and nature of this permeability, and the effect of negatively charged polymers (e. g. teichoic acids) in the wall, has not been clearly defined. The wall is frequently the site of important antigenic material; for example, in many cases it has been shown, that group- or type-specific antigens are located in the outer structures of the cell, including the wall. Consequently, a better understanding of the immunological properties of bacteria, and particularly such features as patho-genicity, require a full understanding of the structure, function and biosynthesis of wall components.


1968 ◽  
Vol 243 (11) ◽  
pp. 3169-3179 ◽  
Author(s):  
D J Tipper ◽  
J L Strominger

1981 ◽  
Vol 256 (17) ◽  
pp. 9229-9234
Author(s):  
E Benedetti ◽  
B Di Blasio ◽  
V Pavone ◽  
C Pedone ◽  
C Toniolo ◽  
...  

1970 ◽  
Vol 245 (14) ◽  
pp. 3675-3682
Author(s):  
Roland Plapp ◽  
Jack L. Strominger

1966 ◽  
Vol 116 ◽  
pp. 487-515 ◽  
Author(s):  
John S. Anderson ◽  
Pauline M. Meadow ◽  
Mary A. Haskin ◽  
Jack L. Strominger

1991 ◽  
Vol 260 (1) ◽  
pp. R126-R133 ◽  
Author(s):  
L. Johannsen ◽  
J. Wecke ◽  
F. Obal ◽  
J. M. Krueger

Muramyl peptides have a variety of biological effects in mammals, including enhancement of the immune response, sleep, and body temperature. Although mammals lack biosynthetic pathways for muramyl peptides, they are found in mammals and are well known as components of bacterial cell walls. This suggests that phagocytic mammalian cells digest bacterial cell walls and produce biologically active muramyl peptides. Staphylococcal cell walls were radioactively labeled during growth of the bacteria. During the digestion of these radiolabeled bacteria, murine bone marrow macrophages produced low-molecular-weight substances that coeluted chromatographically with the radioactive cell wall marker. Further separation of these substances using reversed-phase high-performance liquid chromatography resulted in the isolation of substances with high specific biological activity. Intracerebroventricular injection of rabbits with these substances induced an increase in slow-wave sleep and body temperature and a suppression of rapid-eye-movement sleep. The characteristics of the biological responses and the chromatographic behavior of the active components are consistent with those of muramyl peptides. The ability of macrophages to tailor muramyl peptides from peptidoglycan may provide an amplification step for the immune response. Muramyl peptides released by macrophages may also act as mediators for various facets of the acute phase response elicited by bacterial infections such as fever and sleep.


1982 ◽  
Vol 38 (3) ◽  
pp. 817-824 ◽  
Author(s):  
T Ogawa ◽  
S Kotani ◽  
K Fukuda ◽  
Y Tsukamoto ◽  
M Mori ◽  
...  

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