The first milk substitute for giant panda cubs was developed in 1988 based on limited data about giant panda breast milk and that of certain types of bear. Mixtures of other formulas have also been fed to cubs at some facilities. However, they are not of sufficient nutritional quality for promoting growth in panda cubs. Here, we report analysis of giant panda breast milk and propose new milk substitutes for cubs, which were developed based on the results of our analysis. The Chengdu Research Base of Giant Panda Breeding obtained breast milk samples from three giant pandas. Up to 30 ml of breast milk were collected from each mother by hand. Then, the milk samples were frozen and sent to Nihon University. The levels of protein, fat, carbohydrates, ash, moisture, vitamins, minerals, total amino acids, fatty acids, lactose and other carbohydrates in the milk were analyzed. The breast milk samples exhibited the following nutritional values: protein: 6.6–8.5%, fat: 6.9–16.4%, carbohydrates: 2.5–9.1%, ash: 0.9–1.0% and moisture: 67–83%. We designed two kinds of milk substitutes based on the data obtained and the nutritional requirements of dogs, cats and rodents. The nutritional composition of the milk substitutes for the first and second stages was as follows: protein: 38 and 26%, fat: 40 and 40%, carbohydrates: 13 and 25%, ash: 6 and 6% and moisture: 3 and 3%, respectively. In addition, the substitutes contained vitamins, minerals, taurine, docosahexaenoic acid, lactoferrin, nucleotides and other nutrients.
Hand-reared elephant calves that are nursed with milk substitutes sometimes suffer bone fractures, probably due to problems associated with nutrition, exercise, sunshine levels and/or genetic factors. As we were expecting the birth of an Asian elephant (Elephas maximus), we analyzed elephant’s breast milk to improve the milk substitutes for elephant calves. Although there were few nutritional differences between conventional substitutes and elephant’s breast milk, we found a large unknown peak in the breast milk during high-performance liquid chromatography-based amino acid analysis and determined that it was glucosamine (GlcN) using liquid chromatography/mass spectrometry. We detected the following GlcN concentrations [mean ± SD] (mg/100 g) in milk hydrolysates produced by treating samples with 6M HCl for 24 hr at 110°C: four elephant’s breast milk samples: 516 ± 42, three cow’s milk mixtures: 4.0 ± 2.2, three mare’s milk samples: 12 ± 1.2 and two human milk samples: 38. The GlcN content of the elephant’s milk was 128, 43 and 14 times greater than those of the cow’s, mare’s and human milk, respectively. Then, we examined the degradation of GlcN during 0–24 hr hydrolyzation with HCl. We estimated that elephant’s milk contains >880 mg/100 g GlcN, which is similar to the levels of major amino acids in elephant’s milk. We concluded that a novel GlcN-containing milk substitute should be developed for elephant calves. The efficacy of GlcN supplements is disputed, and free GlcN is rare in bodily fluids; thus, the optimal molecular form of GlcN requires a further study.
We examined the effects of orally administered lactoferrin (LP) on cytokine productions of spleen cells. Spleen cells from BALB/c mice were cultured with concanavalin A 1 to 4 days after the oral administration of bovine LP. Concentrations of IFN-y in the supernatants were enhanced by LP feeding, while those of IL-4 were not. In contrast to LP, an oral administration of p'-lactoglobulin or pepsin hydrolysate of LP failed to show the enhancement. When stimulated by anti-CD3 antibody, IPN-»y production by CD4+ T cells fractionated from spleen cells was augmented by the oral administration of LP. On the other hand, in response to lipopolysaccharide (LPS), spleen cells from the mice fed LP secreted enhanced levels of IL-10. Levels of IFN-"y secretion from the spleen cells were not affected. While IL-10 production in response to LPS by CD1lc+ cells from spleen cells was promoted by LP feeding, the cytokine secretion from CD1lb+ cells was not affected. These results indicate that enterally administered LP affects the host immune responses by modulating cytokine responses, and suggest a possible clinical application of LP as a drug for immune modulator.
The structures of the N- and O-linked sugar chains of recombinant human macrophage colony-stimulating factor (rhM-CSF) from Chinese hamster ovary (CHO) cells were studied. rhM-CSF is a homodimeric glycoprotein. Sugar composition analysis revealed that rhM-CSF contained 4.1 mol N-acetylgalactosamine, 10.3 mol N-acetylglucosamine, 5.0 mol mannose, 10.0 mol galactose, 1.4 mol fucose, and 11.8 mol sialic acid per mol of the monomer. The N- and O-linked sugar chains liberated by hydrazinolysis were N-acetylated, and the reducing-end sugar residues were tagged with 2-aminopyridine. The pyridylamino (PA-) sugar chains thus obtained were purified by HPLC. The structures of the PA-sugar chains were analyzed by a combination of reversed-phase and size-fractionation HPLC, and exoglycosidase digestions, from which the structures of the rhM-CSF sugar chains were estimated to be as follows: monosialo biantennary sugar chain (9 mol%), monosialo fucosylbiantennary sugar chain (10 mol%), disialo biantennary sugar chain (30 mol%), disialo fucosylbiantennary sugar chain (28 mol%), disialo triantennary sugar chain (7 mol%), trisialo triantennary sugar chain (11 mol%), and trisialo fucosyltriantennary sugar chain (5 mol%) for the N-linked sugar chains, and asialo (27 mol%), monosialo (51 mol%), and disialo (22 mol%) Galbeta1-3GalNAc for the O-linked sugar chains. Sialic acid residues were linked to the N-linked sugar chains through an alpha2-3 linkage.
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