Cellular changes during boron-deficient culture of the diatom Cylindrotheca fusiformis

The effects of boron-deficient culture were studied on the unicellular diatom. Cylindrotheca fusiformis Reimann and Lewin. After 24 to 30 h, cell division was almost completely inhibited in boron-deficient cultures. By 48 h of culture, boron-deficient diatoms had approximately twice the modal cell volume of control cells, and at least twice the amount of organic constituents such as protein (2.0x), insoluble carbohydrate (2.4x), total phenols (2.6x), and chlorophyll at (2.1x). Boron deficiency led to irreversible damage after this time.
Dark respiration was 1 nmol O₂/min × 10⁶ cells for both control and boron-deficient diatoms prior to 40 h of culture. By 48 h, the respiratory rate of boron-deficient diatoms was double that of controls. The proportion of ¹⁴C-glucose metabolized by the pentose phosphate pathway was similar in both control and boron-deficient diatoms after 24 and 48 h of culture. After 24 h, the in vitro activity of glucose-6-phosphate dehydrogenase was similar in both control and boron-deficient cells, although the pool size of its substrate, glucose-6-phosphate, was 26% greater in boron-deficient cells. The cellular amount of glucose-6-phosphate dehydrogenase continued to increase once mitosis was arrested in boron-deficient diatoms. Boric acid (1 mM) inhibited 6-phosphogluconate dehydrogenase by 18% in diatom homogenates.
During the early stages of boron deficiency, the uptake of silicate, nitrate, and phosphate, and the in vitro activity of β-glucosidase were similar to control diatoms. After cell division was inhibited, boron-deficient diatoms accumulated more nitrate and phosphate, and retained a higher level of β-glucosidase than control cells.     

ATP synthesis in lettuce seeds during ripening

During the ripening of lettuce seeds, ATP, AMP + ADP, and moisture decrease to very low levels, and the ability to produce ATP from AMP + PEP (phosphoenolpyruvate) and the PEP-carboxylase (EC 4.1.1.38) activity is diminished. Malate dehydrogenase (EC 1.1.1.37) and pyruvate kinase (PK) (EC 2.7.1.40) decreased up to 10 days after anthesis, after which a sharp increase occurred.     

Human liver aldehyde dehydrogenase in Chinese and Asiatic Indians: Gene deletion and its possible implications in alcohol metabolism

Two separate human liver aldehyde dehydrogenases exist which show differences in substrate specificity, cation inhibition or activation, and molecular weight. In this paper we report a common absence of enzyme 2 in Chinese which may be taken to indicate a gene deletion coding for this enzyme. The possible implication of this gene deletion among Chinese is discussed.     

A mutation affecting the lactate dehydrogenase locus Ldh-1 in the mouse—I. Genetical and electrophoretical characterization

(101/El × C3H/El)F₁ male mice were injected intraperitoneally with the mutagen procarbazine hydrochloride and immediately caged with untreated test-stock females. Crude liver extracts from the offspring were subjected to polyacrylamide gel isoelectric focusing, and the gels were stained for six enzymes. In the experimental group (mutagen treated spermatogonial germ-cell stage), a dominant inherited banding alteration of the lactate dehydrogenase (LDH) pattern was detected. By crossing the heterozygous mutants, homozygotes were obtained that showed much less gel staining intensity. The mutation is codominantly expressed with 100% penetrance. The banding alteration was also observed in muscle, kidney, heart, blood, brain, testis, spleen, and lung. Polyacrylamide gel electrophoresis was performed with all the tissues examined. The mutation causes the intensity of the band corresponding to LDH-A (primary molecular form in muscle) to decrease from that of the wild type, while the intensity of the bands corresponding to LDH-B (primary molecular form in heart) remains constant. It is concluded that the mutation affects the locus coding for LDH of the muscle type. Ldh-1 ^c is proposed as the allele symbol.     

Genetic control of lactate dehydrogenase isozymes in Paramecium caudatum

The LDH isozymes were surveyed in bacterized cultures of syngens 1, 3, 12, and 13 of Paramecium caudatum by polyacrylamide gel electrophoresis. All the examined stocks of different syngens except one stock in syngen 3 had a single common LDH isozyme, and intra- and intersyngenic variation was not observed except for the one stock in syngen 3. Breeding data using the exceptional stock indicated that the LDH isozymes of P. caudatum are controlled by two codominant alleles at a single locus whose products aggregate randomly, forming a dimer.     

Assignment of the sorbitol dehydrogenase locus to human chromosome 15 pter→q21

The locus for sorbitol dehydrogenase (SORD, E.C. 1.1.1.14) has been shown to segregate with hexosaminidase A and mannose phosphate isomerase in a series of human-Chinese hamster somatic cell hybrids. Cytogenetic analysis supports the assignment to chromosome 15 and further defines the gene locus to the region 15pterq21.This research was supported by the Medical Research Council of Canada (MT 4061), the Children's Hospital of Winnipeg Research Foundation, Inc., and the Department of Health, Province of Manitoba (H.S.W.).     

Ectoprotein kinase activity of the isolated rat adipocyte.

Intact adipocytes exhibit ectoprotein kinase activity as reflected by their ability to catalyze the transfer of the terminal phosphate of (γ-³²P) ATP to histone added to a cell suspension. This activity is substrate, time and cell number dependent. Lineweaver-Burk plots gave Km and Vmax values for ATP of 5 × 10^?5 M and 7.14 pmoles/min/1.5 × 10⁵ cells. Cyclic AMP but not cyclic GMP in μM concentrations stimulates ectoprotein kinase activity. The controlled tryptic digestion of intact cells results in reduction of ectoprotein kinase activity. This activity is not due to leakage of intracellular protein kinases during the preparative procedure nor to penetration of histone into the cells. Additional phosphoproteins not accessible to endogenous protein kinase activity are also localized on the external surface of the intact fat cell.     

Algal oxidation of aromatic hydrocarbons: formation of 1-naphthol from naphthalene by Agmenellum quadruplicatum, strain PR-6.

Hydroxyurea induces repair replication in human lymphoblastoid NC37 BaEV cells during incubation with liver microsomes and NADPH. Catalase reduces hydroxyurea-induced repair by more than 95%, suggesting that hydrogen peroxide derived from hydroxyurea in the presence of the metabolic activation system is involved in the DNA damage.