A new heredity counseling service in Western Canada

ANIMAL GENETICS: Frederick B. Hutt. The Ronald Press Company, New York, 1964. 546 pp., $12.00.

INTERNATIONAL POPULATION CONFERENCE —CONCRAGES INTERNATIONAL DE LA POPULATION, OTTAWA, 1963: International Union for the Scientific Study of Population, Liège, 1964, 468 pp.

PROCEEDINGS OF THE 34TH SESSION, OTTAWA, 1963: Bulletin of the International Statistical Institute, Volume XL, Book 1, Toronto, 1964, pp. 319–494: Joint meetings with the International Union for the Scientific Study of Population.

THE CONCEPT OF RACE: Ashley Montagu, editor. Free Press of Glencoe, New York, 1964. 270 pp., $5.95.

PREGNANCY, CONCEPTION AND HEREDITY: Eric Weiser (Translated from the German by Therese Pol; So ensteht der Mensch: Von Zeugung und Vererbung, Ullstein Bücher, 1959). Blaisdell Publishing Co., New York, 1965. 148 pp., $1.50.     

Abstracts

BIOFEEDBACK AND SELF‐CONTROL, 1970. Edited by Theodore Barber, Leo V. Di‐Cara, Joe Kamiya, Neal E. Miller, David Shapiro, and Johann Stoyva. Aldine Press, Chicago, 1971. 546 pp. $12.00.

INSANITY AND IDIOCY IN MASSACHUSETTS. REPORT OF THE COMMISSION ON LUNACY, 1855: By Edward Jarvis. Harvard University Press, Cambridge, Mass., 1971. 213 pp. $9.00.

METRIC TRENDS IN HOMINID DENTAL EVOLUTION: By Milford H. Wolpoff. Studies in Anthropology No. 2, Case Western Reserve University Press, Cleveland, 1971. 244 pp. $5.95.

CULTURE AND POPULATION: A COLLECTION OF CURRENT STUDIES: Edited by Steven Polgar. Carolina Population Center, Chapel Hill, North Carolina, 1971. 19S pp. $1.50, paperback.

AN INTRODUCTION TO ANTHROPOLOGY: By Ralph L. Beals and Harry Hoijer. Fourth Edition. The Macmillan Company, New York, 1971. 711 pp. $10.95.

CARMICHAEL'S MANUAL OF CHILD PSYCHOLOGY. Edited by Paul H. Mussen. John Wiley and Sons, Inc., New York, 1970. Two vols: Vol. 1, 1519 pp., $30.00; Vol. 2, 782 pp., $20.00. The set: $40.00.

MATHEMATICAL TOPICS IN POPULATION GENETICS: Edited by Ken‐ichi Kojima. Springer‐Verlag. New York, 1970. 400 pp. $18.70.

AMERICAN DAWN. A NEW MODEL OF AMERICAN PREHISTORY: By Louis A. Brennan. MacMillan, New York, 1970. 390 pp. $8.95.

PROGRESS IN MEDICAL GENETICS: Edited by Arthur G. Steinberg and Alexander G. Bearn. Vol. 7. Grune and Stratton, New York, 1970. 243 pp. $16.50.

CONGENITAL MALFORMATIONS: Edited by F. Clarke Fraser and V. A. McKusick. Excerpta Medica, Amsterdam, New York, 1970. 450 pp. $27.00.

THE HUMAN PLACENTA: By J. D. Boyd and W. J. Hamilton, W. Heffer and Sons Ltd., Cambridge, 1970. 365 pp. $43.83.

DENTAL HEALTH EDUCATION: Report of a WHO Expert Committee. World Health Organization Technical Report Series No. 449, World Health Organization, Geneva, 1970. 28 pp. $0.60.

MULTIPURPOSE SEROLOGICAL SURVEYS AND WHO SERUM REFERENCE BANKS: Report of a WHO Scientific Group. World Health Organization Technical Report Series No. 454. World Health Organization, Geneva, 1970. $1.75. 95 pp.

MENTAL HEALTH OF ADOLESCENTS AND YOUNG PERSONS. REPORT ON A TECHNICAL CONFERENCE: By A. R. May, J. H. Kahn, and B. Cronholm. World Health Organization, Geneva, 1971. 72 pp. $1.75.

BIOLOGICAL RESEARCH IN SCHIZOPHRENIA: Report of a WHO Scientific Group. World Health Organization, Geneva, 1970. 35 pp. $1.00.

EVOLUTION BY GENE DUPLICATION: By Susumu Ohno. Springer‐Verlag, New York‐Heidelberg‐Berlin, 1970. 160 pp. Hard cover, $9.90.

SYMBIOSIS. ORGANISMS LIVING TOGETHER: By Thomas C. Cheng. Pegasus, New York, 1970. 250 pp. $6.95 ($2.25, paperback).

MARIHUANA RECONSIDERED: By Lester Grinspoon. Harvard University Press, Cambridge, Mass. 1971. 443 pp. $9.95.

THE KHANNA STUDY: POPULATION PROBLEMS IN THE RURAL PUNJAB: By John B. Wyon and John E. Gordon. Harvard University Press, Cambridge, 1971. 437 pp. $14.00.     

Letters

BIOCHEMICAL INDIVIDUALITY: THE BASIS FOR THE GENETOTROPHIC CONCEPT: Roger J. Williams, John Wiley &; Sons, New York, 1956, 214 pp.

THE BIOLOGICAL BASIS OF HUMAN FREEDOM: Theodosius Dobzhansky, Columbia University Press, New York 1956, 139 pp.

COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY, Volume XX, Population Genetics: The Nature and Causes of Genetic Variability in Populations. The Biological Laboratory, Cold Spring Harbor, L. I., New York, 1955, 346 pp.

HERITABLE DISORDERS OF CONNECTIVE TISSUE. Victor A. McKusick, Mosby Co., St. Louis, 1956, 224 pp. $7.50.

THE CHEMICAL BASIS OF HEREDITY: Edited by William D. McElroy and Bentley Glass. The Johns Hopkins Press, Baltimore, 1957, 848 pp.

THE POPULATION OF JAMAICA: George W. Roberts, Cambridge University Press, Cambridge, 1957.     

Distribution of genes affecting characteristics of the population

THE CHANGING POPULATION OF THE UNITED STATES: Conrad Taeuber and Irene B. Taeuber. A Volume in the Census Monograph Series. John Wiley and Sons, Inc., New York; Chapman and Hall, Limited, London; for the Social Science Research Council in cooperation with the U. S. Department of Commerce, Bureau of the Census; 1958; xi, 357 pp.; $7.75.

VARIABLES RELATED TO HUMAN BREAST CANCER: Elving Anderson, Harold J. GOODMAN and SHELDON C. REED. University of Minnesota Press, Minneapolis, 1958, 172 pp., 41 text, tables, 53 appendix tables, 7 figures. $4.00.

THE POPULATION AHEAD, Edited by Roy G. Francis. University of Minnesota Press, Minneapolis, 1958, x, 160 pp.

ABORTION IN THE UNITED STATES: Mary Calderone, M. D. (Editor). Hoeber‐Harper, New York, 1958, 224 pp. $5.50.

DIFFERENTIAL PSYCHOLOGY: Anne Anastasi. The Macmillan Company, New York, 1958 (3rd Edition), 664 pp + xii.

FIVE YEARS OF FAMILY PLANNING IN THE COUNTRYSIDE: Baljit Singh. J. K. Institute Monograph No. 6, J. K. Institute of Sociology &; Human Relations, Lucknow University. 1958. 118 pp.

POPULATION; AN INTERNATIONAL DILEMMA. A Summary of the Proceedings of the Conference on Population Problems— 1956–1957. Frederick Osborn. New York, Population Council, 1958. Pp. ix + 97. $2.00.     

Genetic‐hygienic impairment through incestuous matings

THE EFFECT OF EXPOSURE TO THE ATOMIC BOMBS ON PREGNANCY TERMINATION IN HIROSHIMA AND NAGASAKI: J. V. Neel and W. J. Schull, Publication No. 461, National Academy of Sciences—National Research Council, Washington, 1956, 241 pp., $2.00.

DEMOGRAPHIC ANALYSIS: SELECTED READINGS: Edited by Joseph J. Spengler and Otis Dudley Duncan. The Free Press, Glencoe, Illinois, 1956. xvi, 820 pp. $9.50.

POPULATION THEORY AND POLICY: SELECTED READINGS: Edited by Joseph S. Spengler and Otis Dudley Duncan. The Free Press, Glencoe, Illinois, 1956. x, 522 pp. $7.50.

HEALTH AND DEMOGRAPHY: Halbert L. Dunn; U. S. Department of Health, Education, and Welfare, Public Health Service, Bureau of State Services, National Office of Vital Statistics; Washington, October, 1956, 94 pp., $.50.

SOCIAL CHARACTERISTICS OF URBAN AND RURAL COMMUNITIES, 1950: Otis Dudley Duncan and Albert J. Reiss, Jr., John Wiley and Sons, Inc., New York, 1956, XVIII + 421 pp. $6.50.

THE PSYCHOLOGY OF HUMAN DIFFERENCES: Leona E. Tyler. 2nd Edition. New York, Appleton‐Century‐Crofts, 1956. pp. VIII + 562.     

The fertility of a sample of American elites

THE HUMAH CONDITION. HOW DID WE GET HERE AND WHERE ARE WE GOING?: By Frederick Osborn. Hugh Lauter Levin Associates, New York, 1974. 82 pp.

HUMANISTIC PERSPECTIVES IN MEDICAL ETHICS: Edited by Maurice B. Visscher. Prometheus Books, Buffalo, New York, 1972. 310 pp. $11.95.

MAN FOR MAN: A MULTIDISCIPLINARY WORKSHOP ON EFFECTING MAN'S SOCIAL AND PSYCHOLOGICAL NATURE THROUGH COMMUNITY ACTION: Edited by John L. Carleton and Ursula Mahlendorf. Charles C Thomas, Springfield, Illinois, 1973. 355 pp. $10.95.

THE ORIGINS OF LIFE: By Cyril Ponnamperuma. E. P. Dutton, New York, 1972. 215 pp. $7.95.

PARTNERWAHL UND EHE—THEORIE UND PRAXIS: Edited by Hans W. Jürgens. Wissenschaftlicher Verlag Altmann, Hamburg, Germany, 1972. 217 pp.     

Women's opinion about size of family in the Netherlands

HUMAN BLOOD GROUPS AND INHERITANCE: Sylvia Lawler and L. J. Lawler. Harvard University Press, Cambridge, Mass., 1957.

SOUTHERN RACIAL PROGRESS: THE WAVERING COLOR LINE: Thomas J. Woofter. Public Affairs Press, Washington, D. C., 1957, xii, 189 pp., $3.50.

GENETICS: Edgar Altenburg. New York, Holt and Co., 1957, 496 pp., $6.50.     

Book reviews

COHORT FERTILITY: NATIVE‐WHITE WOMEN IN THE UNITED STATES: P. K. Whelpton, Princeton University Press, Princeton, 1954, XXV + 492 pp. $6.00.

COLONIAL DEVELOPMENT AND POPULATION IN TAIWAN: George W. Barclay, Princeton University Press, Princeton, New Jersey, 1954, xviii, 274 pp., $5.00.     

Book reviews

A METHODOLOGICAL, PSYCHIATRIC AND STATISTICAL STUDY OF A LARGE SWEDISH RURAL POPULATION: Acta Psychiatric et Neurologica Scandinavica Supplementum 89, Tage Larsson and Torsten Sjögren; Donald Burton, Translator; Ejnar Munksgarrd, Copenhagen, 1954, 250 pp.

GENETICS, BIOLOGICAL INDIVIDUALITY AND CANCER: Clarence C. Little, Stanford University Press, Stanford, California, 1954, ix, 115 pp., 27 figures, $2.50.     

Antitumor Activities and Immunochemical Properties of the Cell-wall Polysaccharides from Aureobasidium pullulans

Delipidated cell walls from Aureobasidium pullulans were fractionated systematically.

The cell surface heteropolysaccharide contains D-mannose, D-galactose, D-glucose, and D-glucuronic acid (ratio, 8.5:3.9:1.0:1.0). It consists of a backbone of (1→6)-α-linked D-mannose residues, some of which are substituted at O-3 with single or β-(1→6)-linked D-galactofuranosyl side chains, some terminated with a D-glucuronic acid residue, and also with single residues of D-glucopyranose, D-galactopyranose, and D-mannopyranose.

This glucurono-gluco-galactomannan interacted with antiserum against Elsinoe leucospila, which also reacted with its galactomannan, indicating that both polysaccharides contain a common epitope, i.e., at least terminal β-galactofuranosyl groups and also possibly internal β-(1→6)-linked galactofuranose residues.

It was further separated by DEAE-Sephacel column chromatography to gluco-galactomannan and glucurono-gluco-galactomannan.

The alkali-extracted β-D-glucan was purified by DEAE-cellulose chromatography to afford two antitumor-active (1→3)-β-D-glucans. One of the glucans (M_r, 1–2 × 10⁵) was a O-6-branched (1→3)-β-D-glucan with a single β-D-glucosyl residue, d.b., 1/7, and the other (M_r, 3.5–4.5 × 10⁵) had similar branched structure, but having d.b., 1/5. Side chains of both glucans contain small proportions of β-(1→6)-and β-(1→4)-D-glucosidic linkages.     

Effects of Acetylation with Acetic Anhydricle

1. L-Asparaginase (EC 3.5.1.1) from Escherichia coli A–l–3 was acetylated using acetic anhydride as a modifying chemical. The fully acetylated L-asparaginase retained 60% of the activity of the unmodified L-asparaginase.

2. The acetylated L-asparaginase hydrolyzed D-asparagine and L-glutamine as well as L-asparagine in the same ratio as the unmodified L-asparaginase did.

3. However, the effects of pH on the activity of the acetylated L-asparaginase showed very interesting differences from that of L-asparaginase. On the other hand, both L-asparaginase and the acetylated L-asparaginase exhibited similar pH activity curves on L-glutamine hydrolysis.

4. The acetylated L-asparaginase was found to become more stable against acid or heat in the presence of L-aspartate than in its absence in the same manner as L-asparaginase was.

     

Branched Chain Amino Acid Aminotransferase of Pseudomonas sp

Branched chain amino acid aminotransferase was partially purified from Pseudomonas sp. by ammonium sulfate fractionation, aminohexyl-agarose and Bio-Gel A-0.5 m column chromatography.

This enzyme showed different substrate specificity from those of other origins, namely lower reactivity for l-isoleucine and higher reactivity for l-methionine.

Km values at pH 8.0 were calculated to be 0.3 mm for l-leucine, 0.3 mm for α-ketoglutarate, 1.1 mm for α-ketoisocaproate and 3.2 mm for l-glutamate.

This enzyme was activated with β-mercaptoethanol, and this activated enzyme had different kinetic properties from unactivated enzyme, namely, Km values at pH 8.0 were calculated to be 1.2 mm for l-leucine, 0.3 mm for α-ketoglutarate.

Isocaproic acid which is the substrate analog of l-leucine was competitive inhibitor for pyridoxal form of unactivated and activated enzymes, and inhibitor constants were estimated to be 6 mm and 14 mm, respectively.     

Elimination,Replacement and Isomerization Reactions by Intact Cells Containing Tyrosine Phenol Lyase

Tyrosine phenol lyase catalyzes a series of α,β-elimination, β-replacement and racemization reactions. These reactions were studied with intact cells of Erwinia herbicola ATCC 21434 containing tyrosine phenol lyase.

Various aromatic amino acids were synthesized from l-serine and phenol, pyrocatechol, resorcinol or pyrogallol by the replacement reaction using the intact cells. l(d)-Tyrosine, 3,4-dihydroxyphenyl-l(d)-alanine (l(d)-dopa), l(d)-serine, l-cysteine, l-cystine and S-methyl-l-cysteine were degraded to pyruvate and ammonia by the elimination reaction. These amino acids could be used as substrate, together with phenol or pyrocatechol, to synthesize l-tyrosine or l-dopa via the replacement reaction by intact cells. l-Serine and d-serine were the best amino acid substrates for the synthesis of l-tyrosine or l-dopa. l-Tyrosine and l-dopa synthesized from d-serine and phenol or pyrocatechol were confirmed to be entirely l-form after isolation and identification of these products. The isomerization of d-tyrosine to l-tyrosine was also catalyzed by intact cells.

Thus, l-tyrosine or l-dopa could be synthesized from dl-serine and phenol or pyrocatechol by intact cells of Erwinia herbicola containing tyrosine phenol lyase.     

2-Keto-l-gulonic Acid Fermentation

l-Sorbose metabolism in Pseudomonas aeruginosa IFO 3898 was studied. When the strain was cultivated in l-sorbose medium, l-idonic and 2-keto-l-gulonic acids were detected in the culture broth.

From the results on the metabolism of various sugars and sugar acids with the cell suspension and the metabolites accumulated, the following pathway was proposed for the l-sorbose metabolism in Ps. aeruginosa IFO 3898.

l-Sorbose → l-idose → l-idonic acid → 2-keto-l-gulonic acid.     

2-Keto-l-gulonic Acid Fermentation

A number of bacterial strains from type culture collections and natural sources were examined in their metabolic characteristics toward sorbitol and l-sorbose.

Paper chromatographic analyses of sorbitol and l-sorbose metabolites obtained from the cultures of various bacteria revealed that the organisms producing 2-keto-l-gulonic acid from sorbitol were merely found in the genera Acetobacter, Gluconobacter and Pseudomonas, whereas those producing the acid from l-sorbose were distributed in the twelve genera of bacteria: Acetobacter, Alcaligenes, Aerobacter, Azotobacter, Bacillus, Escherichia, Gluconobacter, Klebsiella, Micrococcus, Pseudomonas, Serratia and Xanthomonas.

G. melanogenus, which was characterized by excellent production of 2-keto-l-gulonic acid from sorbitol, also formed several other sugars and sugar acids as the sorbitol metabolites. These compounds were identified to be d-fructose, l-sorbose, d-mannonic acid, L-idonic acid, 2-keto-d-gluconic acid and 5-keto-d-mannonic acid, respectively, by means of two-dimensional paper chromatography.

Bacteria producing 2-keto-l-gulonic acid from sorbitol were usually isolated from fruits but not from soil.     

Mechanism of Asymmetric Production of d-Amino Acids from the Corresponding Hydantoins by Pseudomonas sp.

The mechanism of asymmetric production of d-amino acids from the corresponding hydantoins by Pseudomonas sp. AJ-11220 was examined by investigating the properties of the enzymes involved in the hydrolysis of dl-5-substituted hydantoins. The enzymatic production of d-amino acids from the corresponding hydantoins by Pseudomonas sp. AJ-11220 involved the following two successive reactions; the d-isomer specific hydrolysis, i.e., the ring opening of d-5-substituted hydantoins to d-form N-carbamyl amino acids by an enzyme, d-hydantoin hydrolase (d-HYD hydrolase), followed by the d-isomer specific hydrolysis, i.e., the cleavage of N-carbamyl-d-amino acids to d-amino acids by an enzyme, N-carbamyl-d-amino acid hydrolase (d-NCA hydrolase).

l-5-Substituted hydantoins not hydrolyzed by d-HYD hydrolase were converted to d-form 5- substituted hydantoins through spontaneous racemization under the enzymatic reaction conditions.

It was proposed that almost all of the dl-5-substituted hydantoins were stoichiometrically and directly converted to the corresponding d-amino acids through the successive reactions of d-HYD hydrolase and d-NCA hydrolase in parrallel with the spontaneous racemization of l-5-substituted hydantoins to those of dl-form.     

Purification and Crystallization of d-Arabinose (l-Fucose) Isomerase from Aerobacter aerogenes by Polyethylene Glycol

d-Arabinose(l-fucose) isomerase (d-arabinose ketol-isomerase, EC 5.3.1.3) was purified from the extracts of d-arabinose-grown cells of Aerobacter aerogenes, strain M-7 by the procedure of repeated fractional precipitation with polyethylene glycol 6000 and isolating the crystalline state. The crystalline enzyme was homogeneous in ultracentrifugal analysis and polyacrylamide gel electrophoresis. Sedimentation constant obtained was 15.4s and the molecular weight was estimated as being approximately 2.5 × 10⁵ by gel filtration on Sephadex G-200.

Optimum pH for isomerization of d-arabinose and of l-fucose was identical at pH 9.3, and the Michaelis constants were 51 mm for l-fucose and 160 mm for d-arabinose. Both of these activities decreased at the same rate with thermal inactivation at 45 and 50°C. All four pentitols inhibited two pentose isomerase activities competitively with same Ki values: 1.3–1.5 mm for d-arabitol, 2.2–2.7 mm for ribitol, 2.9–3.2 mm for l-arabitol, and 10–10.5 mm for xylitol. It is confirmed that the single enzyme is responsible for the isomerization of d-arabinose and l-fucose.     

Bacterial Racemization of α-Amino-ε-caprolactam

1. Several bacteria were isolated from soil which grew on both d- and l-aminolactam and whose cells had an activity to racemize them. They were identified as Achromobacter obae nov. sp., Achr. cycloclastes, Alcaligenes faecalis and Flavobacterium arborescens.

2. Racemization of d- and l-aminolactam was investigated using the lyophilized cells of Achr. obae nov. sp. The optimum pH value of the reaction was about 8.0. The racemizing activity was completely inhibited by 10^?4 m hydroxylamine, and the inhibition was removed by 10^?4 m pyridoxal phosphate. Five percent d- and l-aminolactam solutions were completely racemized with a concomitant slight formation of l-lysine.     

High levels of expression of multiple enzymes in the Smirnoff-Wheeler pathway are important for high accumulation of ascorbic acid in acerola fruits

ABSTRACT

Acerola fruits contain abundant ascorbic acid (AsA). The gene expression levels of three upstream enzymes in the primary AsA biosynthesis pathway were correlated with AsA contents in the fruits of two acerola cultivars. Multiple overexpression of the enzymes increased AsA contents, suggesting their high expression is important for high AsA accumulation in acerola fruits and the breeding of AsA-rich plants.

Abbreviations: AsA: ascorbic acid; PMI: phosphomannose isomerase; PMM: phosphomannomutase; GMP: GDP-d-mannose pyrophosphorylase; GME: GDP-d-mannose 3?,5?-epimerase; GGP: GDP-l-galactose phosphorylase; GPP: l-galactose-1-phosphate phosphatase; GDH: l-galactose dehydrogenase; GLDH: l-galactono-1,4-lactone dehydrogenase     

Studies on d-Glucose-isomerizing Enzyme of Bacillus coagulans,Strain HN-68

Cells of Bacillus coagulans, strain HN-68 grown on the medium containing d-glucose, did not show any measurable d-glucose-isomerizing activity. However, when d-glucose-grown cells were shaked for a few hours in an induction medium containing d-xylose, induced formation of d-glucose-isomerizing enzyme occurred in the cells. Cell weight and number of survival cells showed only an increase of 30 and 10%, respectively during 6 hr induction.

The induced formation of d-glucose-isomerizing enzyme required organic nitrogen such as polypeptone in addition to d-xylose. Development of the maximum activity was observed when the concentration of d-xylose and polypeptone were 2 and 3%, respectively. Initial velocity of induced formation of d-glucose-isomerizing enzyme increased in proportion to the decrease of initial pH values of the induction medium, i.e., at 2 hr induction, activity at pH 4.5 was 5-fold increase than that at pH 8.0.

Induced formation of d-glucose-isomerizing enzyme was inhibited strongly by addition of chloramphenicol, tetracycline, streptomycin, cyanide or azide, and was promoted by threonine plus glycine.