LIGHT BLUE 



178 



LINDERSTR0M-LANG, ET AL 



drops acetic anhydride. Wash with 

 several drops of same. Cover and 

 examine immediately. Cholesterol and 

 its esters violet lilac or red purple, be- 

 coming green. The above two methods 

 abbreviated from Lison (p. 210) are in 

 his excellent judgment specific for 

 cholesterol and its esters if positive. 

 A negative reaction does not definitely 

 prove their absence. See Swyer, G. I. 

 M., Cancer Research, 1942, 2, 372-375 

 for quantitative measurement of the 

 color. 



Light Blue, see Spirit Blue. 



Light Green, see Methyl Green. 



Light Green N, see Malachite Green. 



Light Green SF yellowish (CI, 670) S— acid 

 green, fast acid green N — Commission 

 Certified. This acid di-amino tri- 

 phenyl methane dye is a sulfonated 

 derivative of brilliant green and a 

 valuable counterstain for safranin. It 

 is used by Twort, F. W., Brit. J. Exp. 

 Path., 1924, 5, 350-351 as a double stain 

 with neutral red for animal parasites 

 and microorganisms in tissues. Un- 

 fortunately light green fades quickly. 

 Conn (p. 110) recommends fast green 

 FCF as a substitute. 



Lighting, see Illumination. 



Lignin Pink, a monazo acid dye (British 

 Drug Houses Ltd.). Advised 0.5% aq. 

 solution as a chitin stain and a contrast 

 stain with chlorazol Black E (Cannan, 

 H. G., J. Roy. Micr. Soc, 1941, 61, 

 88-94). 



Lilienfeld-Monti test for phosphorus is not 

 a satisfactory microchemical method. 

 See Bensley's method (R. R., Biol. 

 Bull., 1906, 10, 49-65) and criticism by 

 Lison (p. 118). 



Lillie, see Azure or Toluidin Blue Eosin. 



Lillie's chrom-osmic-acetic fixative. J% 

 aq. chromic acid, 15 cc; 2% aq. osmic 

 acid, 3.5 cc. ; glacial acetic acid, 3 drops. 

 Used by him for echinoderm eggs. 



Lime, see Calcium. 



Linderstr0m-Lang, Kaj. U., and Holier, 

 Heinz, Histochetnical Advances — 

 Written by David Glick, Dept. of 

 Physiological Chemistry, University of 

 Minnesota, Minneapolis 14-, Minn. Octo- 

 ber 17, 1951 — Prof. Linderstr0m-Lang, 

 since 1938 the head of the Department 

 of Chemistry of the Carlsberg Labora- 

 tory, Copenhagen, Denmark, and Dr. 

 Heinz Holter, his associate and head of 

 the Cytochemical Department, are 

 responsible for some of the most sig- 

 nificant advances in the field of quanti- 

 tative histochemistry as well as of 

 protein and proteolytic enzyme chemis- 

 try. Their histochemical work began 

 in 1930 when Dr. Holter came to the 

 Carlsberg Laboratory. Their first ef- 

 forts were directed to the development 



of micro titration techniques that 

 would enable a thousandfold refinement 

 of common macro methods of biochemi- 

 cal analysis without loss of precision. 

 This degree of refinement constituted a 

 temporary compromise since it was 

 their goal to bring reliable quantitative 

 chemical techniques to bear on the 

 study of the single cell, and a hundred 

 thousandfold refinement would be re- 

 quired to achieve this end in the case 

 of mammalian cells. However the one 

 thousandfold refinement did permit 

 work on single microtome sections, 

 protozoa, and ova of certain marine 

 invertebrates. 



The first investigation of the series 

 (Linderstr0m-Lang, K. and Holter, H., 

 Compt. rend. trav. lab. Carlsberg, Ser. 

 Chim., 1931, 19, No. 4) described the 

 micro titration apparatus that was de- 

 vised, (the burettes used were graduated 

 in 0.0002 ml. divisions and readings were 

 taken to 0.00002 ml.) and subsequently 

 Linderstr0m-Lang and Holter adapted 

 the equipment to the measurement of 

 proteolytic enzyme activity. They em- 

 ployed this method for a study of the 

 distribution of peptidase along the roots 

 and sprouts of barley (Linderstr0m- 

 Lang, K. and Holter, H., Ibid., 1932, 

 19, No. 6). When one has developed 

 a new tool it is natural that he employ 

 it for diverse purposes to test its range 

 of usefulness. And accordingly, in the 

 next application of their technique, 

 Holter and Linderstr0m-Lang (Zeit. f. 

 Physiol. Chem., 1932, 219, 223-240) in- 

 vestigated the proteinases of Drosera 

 Rotundi folia, an insectivorous plant, 

 and then Linderstr0m-Lang (Ibid, 1933, 

 215, 167-178) made a study of the pepti- 

 dase content of single eggs of two marine 

 invertebrates, the California sand dollar 

 and Urechis caupo, before and after fer- 

 tilization. These eggs have a wet 

 weight of only about 5 X 10~' g. 



Linderstr0m-Lang and Holter next 

 extended their technique to a method 

 for the iodometric determination of 

 reducing sugars with a precision corre- 

 sponding to 25 X 10~* g. of glucose 

 (Compt. rend. trav. lab. Carlsberg, 

 1933, 19, No. 14), and this was followed 

 by the development of a diffusion 

 method for ammonia sensitive to 14 X 

 10~' g. of nitrogen (Compt. rend. trav. 

 lab. Carlsberg, Ser. Chim., 1933, 19, 

 No. 20.) 



The elegance and general applica- 

 bility to diverse problems of the tech- 

 niques and methods being developed 

 began to attract research workers to 

 the Carlsberg Laboratory from other 

 countries, and the series of publications 

 that had evolved under the heading of 



