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PubMed1993

Polysialosyl glycoconjugates defined by monoclonal antibody M6704 are expressed in human gliomas and embryonic neurons.

The distribution of polysialosyl glycoconjugates defined by a monoclonal antibody M6704 (M6704 antigen) and of its O-acetylated counterpart (O-Ac-M6704 antigen) was investigated in human gliomas and in normal adult and fetal central nervous system. Among 32 gliomas, M6704 antigen was confined to the glioma cell surface and cytoplasmic processes in 21 cases, whereas O-Ac-M6704 antigen was expressed in the Golgi region in 22 cases and at the cell surface in seven cases. In adult tissues M6704 antigen was barely detectable, whereas in fetal tissues it was spatially and temporally expressed at the cell surface and along processes of post-mitotic neurons. The O-Ac-M6704 antigen first appeared in the Golgi regions of neurons at 66 gestational days and increased gradually with further maturation to adult levels. Several polysialoglycoproteins, the most dominant being 51 KD, and C-series polysialogangliosides were isolated from gliomas. These results indicate that M6704 antigen is a distinctive component expressed selectively by embryonic neurons during development and by glioma cells.

Adult↗

PubMed1996

M-cells in the rabbit tonsil exhibit distinctive glycoconjugates in their apical membranes.

The tonsil crypt epithelium contains membranous (M)-cells that transport antigens from the lumen to underlying lymphoid cells, thereby initiating specific immune responses. Mechanisms mediating the adhesion of antigens to the M-cell surface are important for effective and selective uptake of potential pathogens but are still poorly understood. Therefore, the carbohydrates present on crypt epithelial cells of the rabbit palatine tonsil were studied by lectin histochemistry. Ultrathin LR White sections were incubated with a panel of eight lectins conjugated to colloidal gold or biotin. The glycocalyx of the apical membrane of M-cells was selectively labeled by UEA-I, LTA, HPA, and VVA, whereas that of the remaining squamous epithelial cells preferentially bound RCA-I and PNA. WGA and ConA showed only little binding, with no discernible preference for any of the cell types. Double labeling of UEA-1 together with anti-vimentin antibodies revealed that UEA-I-positive epithelial cells also contained the rabbit M-cell marker vimentin, and vice versa. The results show that a specific composition of glycoconjugates, which differs from that on squamous epithelial cells, is found on M-cells of the rabbit tonsil. The M-cell-specific glycoproteins and glycolipids could be selectively targeted by microorganisms that adhere to M-cells and enter the host along this pathway.

Animals↗

PubMed1994

Glycoconjugates mark a transient barrier to neural crest migration in the chicken embryo.

We report that two molecular markers correlate with a transient inhibition of neural crest cell entry into the dorsolateral path between the ectoderm and the somite in the avian embryo. During the period when neural crest cells are excluded from the dorsolateral path, both peanut agglutinin lectin (PNA)-binding activity and chondroitin-6-sulfate (C6S) immunoreactivity are expressed within this path. Both markers decline as neural crest cells enter. Moreover, both markers are absent after an experimental manipulation that accelerates neural crest entry into this path. Specifically, dermamyotome deletions abolish expression of both markers and allow neural crest cells to enter the dorsolateral path precociously. After partial deletions, dermatome remnants remain. These remnants retain PNA and C6S labeling and impede migration locally. Local glycoconjugate expression thus correlates directly with avoidance responses. Since both PNA-binding activity and C6S expression also typify inhibitory somitic tissues, molecules indicated by these markers (or co-regulated molecules) are likely to inhibit both neural crest and axon advance.

Animals↗

PubMed2003

[Functional glycoconjugates involved in cellular interaction].

We first examined the involvement of the complex sphingolipids in cell-substratum adhesion using GM-95, a mutant cell line deficient in glycosphingolipids (GSLs) due to the lack of ceramide glucosyltransferase activity. We determined the adhesion of the mutant cells and stable transfectants expressing GSLs, which were established by transfection of GlcT-1 cDNA into GM-95 cells under neutral sphingomyelinase (sm) treatment. We confirmed that complex sphingolipids play critical roles in cell-substratum adhesion, and the presence of either GSLs or SM is sufficient for the adhesion. We also investigated intracellular signaling (glycosignaling) mediated by endogenous GM1a involved in the neuronal differentiation of PC12 cells using the cholera toxin B subunit (CTB) that specifically binds to ganglioside GM1a. Treatment with CTB induced neuron-like differentiation of PC12 cells. Biochemical analyses demonstrated that the tyrosine phosphorylation induced by CTB was responsible for neuron-like differentiation of PC12 cells and that the MEK-ERK cascade is a part of the biological signals mediated by endogenous ganglioside GM1a on PC12 cells. We further demonstrated that glycosignaling is mediated through a high-affinity ligand, PSGL-1, for P-selection on neutrophils. In this case, engagement of PSGL-1 on the cell surface strongly induced tyrosine phosphorylation of several cellular proteins including ERKs and activated a canonical MAP kinase pathway. Tyrosine phosphorylation induced by engagement of PSGL-1 is responsible for the secretion of interleukin-8 from neutrophils, suggesting that PSGL-1-mediated glycosignals are involved in the progression of the inflammatory response. In this review, we mainly discuss the biological and pathological significance of glycoconjugates in relation to the above issues.

Animals↗

PubMed1989

Alterations in glycoconjugate expression following malignant transformation of human oropharyngeal squamous mucosa.

Malignant transformation of the squamous mucosa in the human oropharynx may be accompanied by alterations in carbohydrate production. Glycoconjugate expression was assessed by examining lectin-binding patterns and ABH isoantigen expression in human biopsy specimens from nine cases of carcinoma in situ and ten cases of invasive squamous cell carcinoma as well as adjacent normal squamous mucosa. Ten different fluorescein-conjugated lectins were used. Each lectin binds to specific nonreducing end-terminal carbohydrate residues. Wheat germ agglutinin and peanut agglutinin displayed intense cytoplasmic and/or membrane binding in more than 90% of the carcinoma in situ and squamous cell carcinoma specimens. However, only 40% of normal squamous epithelium specimens displayed intense cytoplasmic and/or membrane binding with wheat germ agglutinin and peanut agglutinin. Bandieraea simplicifolia I and Helix pomatia exhibited weak binding in less than 35% of normal and neoplastic tissues. Weak canavalia ensiformis binding was identified infrequently in the superficial layers of normal squamous mucosa, but was not found in neoplastic epithelium. None of the cases displayed binding for Dolichos biflorus, Ulex europaeus I, Sophora japonica, Glycine maximus, or Ricinus communis. Monoclonal antibodies directed against ABH blood group isoantigens showed increased cytoplasmic immunoreactivity for anti-H in dysplastic and neoplastic tissues, when compared with normal squamous mucosa. These findings indicate that wheat germ agglutinin and peanut agglutinin and H isoantigen are useful markers of malignancy in squamoproliferative lesions of the oropharynx, apparently reflecting alterations in expression of N-acetyl-D-glucosamine and galactose-related sugars, which appear following malignant transformation.

ABO Blood-Group System↗

PubMed2000

Lectin-binding capacity of glycoconjugates in Escherichia coli 09:K103:NM, 987P+ST+-infected porcine lower small intestines.

Composition of glycoconjugates were investigated in Escherichia coli 09:K103:NM, 987P+ST+-infected lower small intestines of 1-week-old pigs by the use of twenty one biotinylated-labelled lectins with avidin-biotin-peroxidase complex method. Piglets with experimental group were inoculated by feeding 5 ml of culture inoculum (5 x 10(9) colony-forming units/ml) with 15 ml of milk replacer. At the onset of diarrhea, experimental piglets and time-matched control piglets were euthanatized using electrocution, necropsied, and tested by lectin histochemistry. As compared with control, staining intensity of seven lectins altered in ileal villus brush border and goblet cells of pigs inoculated with the pathogen.

Animals↗

PubMed2003

Lectin histochemistry for glycoconjugates in the small intestines of piglets naturally infected with Isospora suis.

Composition of glycoconjugates was examined in small intestines naturally infected with Isospora suis in preweaned pigs by use of 21 biotinylated-labeled lectins with avidin-biotin-peroxidase complex method. As compared with control pig, staining of 18 lectins altered in jejunal villus brush border and goblet cells of pigs naturally infected with I. suis. These results indicate that I. suis infection alters carbohydrate residues on the jejunal intestines.

Animals↗

PubMed2002

Identification and characterization of the peptidic component of the immunomodulatory glycoconjugate Immunoferon.

Inmunoferon is a glycoconjugate of natural origin, formed by the noncovalent association of a protein from Ricinus communis and a polysacharidic moiety, and endowed with immunomodulatory as well as pharmacological activities. This study investigated the nature of polypeptidic component of Inmunoferon. Through biochemical procedures and comparison with protein databases, the isolated protein was identified as the processed form of the seed of Ricinus communis 2S storage polypeptide, which has been termed RicC3. Further analysis of the isolated protein has revealed that it is composed of two different subunits, alpha and beta, which form an heterodimer of high stability and resistance to denaturation, acidic pH and proteolytic cleavage. These findings confirm the excellent properties of the product after oral administration and provide additional support for the pharmacological activities of Inmunoferon.

Adjuvants, Immunologic↗

PubMed2006

High-throughput quantitation of metabolically labeled anionic glycoconjugates by scintillation proximity assay utilizing binding to cationic dyes.

Rapid, quantitative methods suited to a large number of samples are required for studies into the determination of disease etiology and in the evaluation of drugs and biological agents. This chapter describes an assay for anionic glycoconjugates (GCs), including glycosaminoglycans, which are major gene products of chondrocytes appearing in the extracellular matrix. The assay utilizes the electrostatic interaction between negatively charged sulfate and carboxyl groups of anionic GCs synthesized and secreted by chondrocytes with the cationic dye Alcian blue, immobilized to scintillant-coated 96-well plates. Metabolic labeling with D-[1, 6-3H (N)]-glucosamine allows all anionic GCs, including cartilage-specific and hyperglycosylated variants of fibronectin, to be quantitated. If Na235SO4 is used for the metabolic labeling instead, only glycosaminoglycans and proteoglycans will be quantitated. The samples are counted using a multi-detector instrument for scintillation proximity assays, such as the Wallac 1450 Microbeta Trilux, designed for detection of samples in 96-well plates and, as such, can be a high-throughput system. The bound anionic GCs can be visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis after quantitation by elution with denaturing buffers. The method can be modified to include predigestion of the sample with a specific lyase, e.g., chondroitinase ABC or testicular hyaluronidase. To separate polyanions from other digested material after ethanol precipitation, the sample can be assayed as described in this chapter for a particular subtype of anionic GC. This assay addresses the need for high-throughput applications in arthritis and other medical and biological problems.

Alcian Blue↗

PubMed2004

Distributional map of the terminal and sub-terminal sugar residues of the glycoconjugates in the prepubertal and postpubertal testis of a subject affected by complete androgen insensitivity syndrome (Morris's syndrome): lectin histochemical study.

In the present research we have investigated the distribution of the sugar residues of the glycoconjugates in the prepubertal and postpubertal testes of a subject with Morris's syndrome (CAIS, Complete Androgen Insensitivity Syndrome). For this purpose a battery of six horseradish peroxidase-conjugated lectins was used (SBA, PNA, WGA, ConA, LTA and UEAI). We have obtained a complete distributional map of the terminal and sub-terminal oligosaccharides in the tunica albuginea, interstitial tissue, lamina propria of the seminiferous tubules, Leydig cells, Sertoli cells, spermatogonia, mastocytes and endothelial cells. Furthermore the present study has shown that a large amount of sugar residues were detectable in the prepubertal and postpubertal testes but that some differences exist with particular regard to the Sertoli cells. The Sertoli cells and the Leydig cells of the retained prepubertal testis of the patient affected by Morris's syndrome were characterized by the presence of alpha-L-fucose, which was absent in the retained prepubertal testis of the normal subjects. Comparing the results on the postpubertal testis with those obtained on the same aged testis of healthy subjects we have demonstrated that alpha-L-fucose in the Sertoli and Leydig cells and D-galactose-N-acetyl-D-galactosamine in the Leydig cells are a unique feature of the subject affected by Morris's syndrome. D-galactose (ss1,3)-N-acetyl-D-galactosamine and sialic acid, which are present in the Leydig cells of the normal testis were never observed in the same cells of the postpubertal testis of the CAIS patient.

Adolescent↗

PubMed2006

Histochemical analysis of glycoconjugates in the domestic cat testis.

The localization and characterization of oligosaccharide sequences in the cat testis was investigated using 12 lectins in combination with the beta-elimination reaction, N-Glycosidase F and sialidase digestion. Leydig cells expressed O-linked glycans with terminal alphaGalNAc (HPA reactivity) and N-glycans with terminal/internal alphaMan (Con A affinity). The basement membrane showed terminal Neu5Acalpha2,6Gal/GalNAc, Galbeta1,3GalNAc, alpha/betaGalNAc, and GlcNAc (SNA, PNA, HPA, SBA, GSA II reactivity) in O-linked oligosaccharides, terminal Galbeta1,4GlcNAc (RCA120 staining) and alphaMan in N-linked oligosaccharides; in addition, terminal Neu5acalpha2,3Galbeta1,4GlcNac, Forssman pentasaccharide, alphaGal, alphaL-Fuc and internal GlcNAc (MAL II, DBA, GSA I-B4, UEA I, KOH-sialidase-WGA affinity) formed both O- and N-linked oligosaccharides. The Sertoli cells cytoplasm contained terminal Neu5Ac-Galbeta1,4GlcNAc, Neu5Ac-betaGalNAc as well as internal GlcNAc in O-linked glycans, alphaMan in N-linked glycoproteins and terminal Neu5Acalpha2,6Gal/ GalNAc in both O- and N-linked oligosaccharides. Spermatogonia exhibited cytoplasmic N-linked glycoproteins with alphaMan residues. The spermatocytes cytoplasm expressed terminal Neu5Acalpha2,3Galbeta1,4 GlcNAc and Galbeta1,3GalNAc in O-linked oligosaccharides, terminal Galbeta1,4GlcNAc and alpha/betaGalNAc in N-linked glycoconjugates. The Golgi region showed terminal Neu5Acalpha2,3Galbeta1,4GlcNac, Galbeta1,4GlcNAc, Forssman pentasaccharide, and alphaGalNAc in O-linked oligosaccharides, alphaMan and terminal betaGal in N-linked oligosaccharides. The acrosomes of Golgi-phase spermatids expressed terminal Galbeta1,3GalNAc, Galbeta1,4GlcNAc, Forssmann pentasaccharide, alpha/betaGalNAc, alphaGal and internal GlcNAc in O-linked oligosaccharides, terminal alpha/betaGalNAc, alphaGal and terminal/internal alphaMan in N-linked glycoproteins. The acrosomes of cap-phase spermatids lacked internal Forssman pentasaccharide and alphaGal, while having increased alpha/betaGalNAc. The acrosomes of elongated spermatids did not show terminal Galbeta1,3GalNAc, displayed terminal Galbeta1,4GlcNAc and alpha/betaGalNAc in N-glycans and Neu5Ac-Galbeta1,3GalNAc in O-linked oligosaccharides.

Acrosome↗

PubMed2007

Histochemical study of glycoconjugates in the toadfish Halobatrachus didactylus oesophagus epithelium.

The carbohydrate expression in the epithelium lining the oesophagus of the toadfish Halobatrachus didactylus was studied by means of conventional and lectin histochemistry. The stratified epithelium was constituted by basal cells, polymorphous cells in the intermediate layer, pyramidal and flattened cells in the outer layer and contained two types of large secretory cells: goblet cells and sacciform cells. PAS, Alcian blue pH 2.5 and pH 1.0 stained very strongly the goblet cells, weakly the surface of the other epithelial cells but did not stain the sacciform cells. The goblet cells cytoplasm contained oligosaccharides with terminal Galbeta1,3GalNAc, alpha/betaGalNAc, Galbeta1,4GlcNAc, alphaL-Fuc and internal betaGlcNAc residues (PNA, SBA, RCA120, UEA I, LTA and KOH-sialidase-WGA affinity). Galbeta1,4GlcNAc, alphaL-Fuc and internal betaGlcNAc were also found in the glycocalyx. The sacciform cells expressed sialyloligosaccharides terminating with Neu5Acalpha2,3Galbeta1,4GlcNac, Neu5Acbeta2,6Gal/GalNAc, Neu5AcForssman pentasaccharide (MAL II, SNA, KOH-sialidase-DBA staining) as well as asialo-glycoconjugates with terminal/internal alphaMan (Con A affinity) and with terminal Galbeta1,3GalNAc, Forssman pentasaccharide, Galbeta1,4GlcNAc, GalNAc (HPA and SBA reactivity), alphaGal (GSA I-B4 reactivity), D-GlcNAc (GSA II labelling), alphaL-Fuc. The basal cells cytoplasm exhibited terminal/internal alphaMan and terminal Neu5Acalpha2,6Gal/GalNAc, Galbeta1,4GlcNAc, alpha/betaGalNAc, alphaGal, GlcNAc, alphaL-Fuc. Intermediate cells showed oligosaccharides with terminal/internal alphaMan and/or terminating with Neu5Acalpha2,6Gal/GalNAc, Galbeta1,4GlcNAc in the cytoplasm and with Neu5Acalpha2,3Galbeta1,4GlcNac, alpha/betaGalNAc, alphaGal, GlcNAc, alphaL-Fuc in the glycocalyx. The pyramidal cells expressed terminal/internal alphaMan and terminal Neu5Acalpha2,6Gal/GalNAc, alpha/betaGalbeta1,4NAc, alphaGal, alphaL-Fuc in the entire cytoplasm, terminal Neu5Acalpha2,3Galbeta1,4GlcNac and Forssman pentasaccharide in the apical extension, internal betaGlcNAc and/or terminal alphaL-Fuc in the luminal surface, Neu5Acalpha2,3Galbeta1,4GlcNac, Neu5Acalpha2,6Gal/GalNAc, Galbeta1,4GlcNAc, alphaGal in the basolateral surface. The flattened cells displayed glycans with terminal/internal alphaMan and terminal Neu5Acalpha2,6Gal/GalNAc, alpha/betaGalNAc, alphaGal, D-GlcNAc in the entire cytoplasm, glycans terminating with Galbeta1,3GalNAc and/or internal betaGlcNAc in the sub-nuclear cytoplasm.

Animals↗

PubMed1988

A new reagent for the preparation of glycoconjugates.

The thioglycoside derivative 2-carbazoylethyl 1-thio-beta-D-galactopyranoside hydrochloride was synthesized. Conversion of the carbazoyl group into the reactive azidocarbonyl function leads to a well suited reagent for the preparation of glycoconjugates via amidation of proteins or synthetic carriers in aqueous media.

Glycoconjugates↗

PubMed1999

Glycoconjugate expression in follicle-associated epithelium (FAE) covering the nasal-associated lymphoid tissue (NALT) in specific pathogen-free and conventional rats.

We examined lectin-histochemically the glycoconjugate expression in the follicle-associated epithelium (FAE) covering the nasal-associated lymphoid tissue (NALT) in the rat under specific pathogen-free (SPF) and conventional (CV) conditions and compared the results for SPF and CV rats as well as for membranous (M) cells and adjacent ciliated respiratory epithelial (CRE) cells in FAE. N-acetylgalactosamine-specific lectins, Dolichos biflorus (DBA), Helix pomatia (HPA), Glycine max (SBA) and Vicia villosa (VVA), and alpha-L-fucose-specific lectin, Ulex europaeus (UEA-I), preferentially bound to M cells mainly in the luminal surface compared with CRE cells in SPF rats, whereas DBA and UEA-I showed signs of preferential binding to the apical and basolateral cytoplasm as well as to the luminal surface of M cells in CV rats. In addition, HPA, SBA and VVA more frequently and extensively labeled M cells than CRE cells in CV rats with the same subcellular staining pattern as DBA and UEA-I. On the whole, the changes in lectin binding frequency and strength were more prominent in M cells than in CRE cells in both SPF and CV rats. The present results indicate that DBA and UEA-I are useful as markers of M cells in NALT. Furthermore, the pattern of expression of carbohydrate residues recognized by such lectins in SPF and CV rats suggests that M cells are highly sensitive to environmental changes.

Animals↗

PubMed1995

Structure, function and biosynthesis of sperm-activating peptides and fucose sulfate glycoconjugate in the extracellular coat of sea urchin eggs.

A decapeptide (GFDLNGGGVG) isolated from the solubilized jelly layer of the sea urchin Hemicentrotus pulcherrimus stimulates the respiration and motility of H. pulcherrimus spermatozoa and, in addition, produces a number of biological effects on H. pulcherrimus spermatozoa including increases in cAMP and cGMP levels, activation of a Na+/H+ exchange system, and increases in intracellular pH (pHi) and [Ca2+] ([Ca2+]i). The peptide activates the metabolism of endogenous phosphatidylcholine and promotes the acrosome reaction as a specific co-factor of a major acrosome reaction-inducing substance, fucose sulfate glycoconjugate. The peptide also induces an electrophoretic mobility change in the guanylate cyclase of the sperm plasma membrane with concomitant dephosphorylation and inactivation of the enzyme. Seventy-four peptides producing similar biological effects, named sperm-activating peptide (SAP), have since been purified from the solubilized jelly layer of seventeen species of sea urchins distributed over five taxonomic orders. These peptides show essentially the same biological effects on sea urchin spermatozoa although their activity and structures are specific at the ordinal level. Equilibrium binding experiments using a radioiodinated SAP-I analogue [GGGY(125I)GFDLNGGGVG] to H. pulcherrimus spermatozoa suggests the presence of two classes of receptors (high affinity and low affinity) specific for SAP-I binding. Based on the Kd values and EC50's for SAP-I's biological activity, we presume that the high affinity receptor is associated with respiration-stimulating activity and elevations in pHi, while the low affinity receptor is coupled to elevations in cGMP and [Ca2+]i. The radioiodinated SAP-I analogue crosslinks to a 71 kDa protein which contains a single membrane-spanning domain at almost near C-terminus. A SAP-I precursor which is synthesized in the accessory cells contains five SAP-I and seven SAP-I-like decapeptides, each separated by a single lysine residue.

Amino Acid Sequence↗

PubMed1998

Compositional changes in glycoconjugates recognized histochemically with lectins in Purkinje cells in suckling and adult rats.

Cerebella from suckling and adult rats were examined histochemically with 19 different biotin-labeled lectins. Purkinje cells from postnatal rats had a marked ability to combine with many lectins, but minimal ability was found in adult rats except for Con-A, LEL, and MAL lectins. The cell body of Purkinje cells on postnatal day 7 was strongly labeled with 6 lectins (Con-A, LTL, MAL, SJA, UEA-I, and VVA). Only moderate staining was observed with these lectins on postnatal day 5. The dendritic tree of the cells showed a moderate labeling ability with LTL and UEA-I on postnatal days 15 and 20. The dendritic tree was strongly labeled with MAL on postnatal days 10, 15, 20 and adult. Positive reactions were observed in the cells when cerebellar sections from rats on postnatal day 7 were incubated with 3 other lectins (AAL, LEL, and SBA). The cells on postnatal day 7 were rarely labeled with BSL-II, DBA, DSL, LCA, PNA, PSA, RCA120, SSA, STL, and WGA. Purkinje cells on postnatal day 7 may be rich in N-linked oligosaccharides, with terminal sugar structures that resemble blood-group-related antigens (type H) and/or tumor-related antigens. These glycoconjugates may be present at low levels in the Purkinje cells of adult rats. Dendrites of Purkinje cells of adult rats were strongly labeled by Con-A, LEL, and MAL. The dendrites of Purkinje cells may be rich in highly branched oligosaccharides.

Animals↗

PubMed2001

Identification of inhibitors of DNA topoisomerase II from a synthetic library of glycoconjugates.

A library of 24 glycoconjugates related to glycosylated beta-amino acid derivative (I) was been prepared and screened against DNA topoisomerase-II of the filarial parasite S. cervi. Among these, compound 6 was found to be a potent inhibitor of DNA topoisomerase-II with 95% inhibition at 1.09 microM. Furthermore, compound 6 was at least three times more potent than the lead compound, glycosylated beta-amino acid derivative I.

Enzyme Inhibitors↗

PubMed2002

Glycoconjugate libraries accessed by multicomponent reactions.

Glycobiology opens a wide field for new therapeutic approaches. However, the complexity and unavailability of various carbohydrate test compounds has excluded this class of natural products from modern screening systems. Alternatively, glycomimetics are considered to be more drug-like candidates for development. By means of multicomponent condensations (MCCs) utilizing suitable carbohydrate synthons, rapid and effective access to glycoconjugate libraries can be obtained. The flexibility of MCCs allows the assembly of diverse carbohydrate containing libraries. It may be assumed that MCCs containing carbohydrate moieties will play an important role in glycomimetic chemistry and biology.

Aldehydes↗