Tách biệt và định tính một phần hai quần thể hạt tiết từ tuyến nước bọt mang tai ở chuột rat

Arneberg P (1971) Quantitative determination of protein in aliva. A comparison of analytical methods. Scand J Dent Res 79:60–64 Bedi KS, Cope GH, Williams MA (1974) An electron microscopic-stereologic analysis of the zymogen granule content of the parotid glands of starved rabbits and changes induced by feeding. Arch Oral Biol 19:1127–1133 Berg NB, Austin BP (1976) Intracellular transport of sulfated macromolecules in parotid acinar cell. Cell Tissue Res 165:215–225 Bernfeld P (1951) Enzymes of starch degradation and synthesis. In: Nord FF (ed) Advances in enzymology, Vol 12: Interscience, New York, pp 379–428 Castle JD, Jamieson JD, Palade GE (1972) Radioautographic analysis of the secretory process in the parotid acinar cell of the rabbit. J Cell Biol 53:290–311 Castle JD, Jamieson JD, Palade GE (1975) Secretion granules of the rabbit parotid gland. Isolation, subfractionation and characterization of the membrane and content subfractions. J Cell Biol 64:182–210 Cooperstein SJ, Lazarow A (1951) A microspectrophotometric method for the determination of cytochrome oxidase. J Biol Chem 189:665–670 Gianattasio G, Zanini A (1976) Presence of sulfated proteoglycans in prolactin secretory granules isolated from the rat pituitary gland. Biochim Biophys Acta 439:349–357 Giannattasio G, Zanini A, Rosa P, Meldolesi J, Margolis RK, Margolis RU (1980) Molecular Organization of prolactin granules III. Intracellular transport of sulfated glycosaminoglycans and glycoproteins of the bovine prolactin granule matrix. J Cell Biol 86:273–279 Itoh T (1977) Quantitative study of secretory granules of the parotid gland acinar cell of the rat. J Electron Microsc 26:19–28 Iversen JM, Johnson DA, Kauffman DL, Keller PJ, Robinovitch MR (1982) Isolation and characterization of the basic prolinerich proteins from rat parotid saliva. Arch Oral Biol 27:925–930 Jamieson JD, Palade GE (1967) Intracellular transport of secretory proteins in the pancreatic exocrine cell. II. Transport to condensing vacuoles and zymogen granules. J Cell Biol 34:597–615 Keller PJ, Robinovitch M, Iversen J, Kauffman DL (1975) The protein composition of rat parotid saliva and secretory granules. Biochim Biophys Acta 379:562–570 Keller PJ, Iversen JM, Kauffman DL, Robinovitch MR (1984) Identification of chondroitin sulfate as a secretory product in rat parotid glands. J Dent Res 63:1180 ABST Kirshner N, Wallach D, Sharoni Y, Schramm M (1973) Purification of secretory granules on a urografin gradient. Anal Biochem 52:589–594 Laemmli UK, Fahre M (1973) Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol 80:575–599 Levine M, Keller PJ (1977) The isolation of some basic proline-rich proteins from human parotid saliva. Arch Oral Biol 22:37–41 Lowry OH, Rosenbrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275 Madsen NP (1969) Use of toluene/triton X-100 scintillation mixture for counting 14C-protein radioactivity. Anal Biochem 29:542–544 Miller GL, Golder RH, Miller EE (1951) Determination of pentoses. Effects of varying proportions of Bial's color reagent. Anal Chem 73:904–915 Palade G (1975) Intracellular aspects of the process of protein synthesis. Science 189:345–358 Peters TJ, Muller M, deDuve C (1972) Lysosomes of the arterial wall 1. isolation and subcellular fractionation of cells from normal rabbit aorta. J Exp Med 136:1117–1139 Reggio HA, Dagorn JC (1978) Ionic interactions between bovine chymotrypsinogen A and chondroitin sulfate. A.B.C. J Cell Biol 78:951–957 Robinovitch MR, Sreebny LM (1969) Separation and identification of some of the protein components of rat parotid saliva. Arch Oral Biol 14:935–949 Robinovitch MR, Sreebny LM, Smuckler EA (1966) Preservation of the secretory granules of rat parotid gland for electron microscopy. Exp Cell Res 42:634–639 Robinovitch MR, Keller PJ, Iversen J, Kauffman DL (1975) Demonstration of a class of proteins loosely associated with secretory granule membranes. Biochim Biophys Acta 382:260–264b Robinovitch MR, Iversen JM, Johnson DA (1979) Differences in proteins of parotid saliva and secretory granule contents. J Dent Res 58:792 ABST Robinovitch MR, Iversen JM, Oberg SG (1980a) Isolation and partial characterization of secretory granule membranes from the rat parotid gland. Arch Oral Biol 25:523–530 Robinovitch MR, Lagunoff D, Iversen JM (1980b) The presence of mast cell granules in rat parotid secretory granule preparations. J Histochem Cytochem 28:1351–1354 Schramm M, Bdolah A (1964) The mechanism of enzyme secretion by the cell. III Intermediate stages in amylase transport as revealed by pulse labelling of slices of parotid gland. Arch Biochem Biophys 104:67–72 Sharoni Y, Eimeral S, Schramm M (1976) Secretion of old versus new exportable proteins in rat parotid slices. J Cell Biol 71:107–122 Wallach D, Schramm M (1971) Calcium and the exportable protein in rat parotid gland. Parallel subcellular distribution and concomitant secretion. Eur J Biochem 21:433–437 Weber K, Osborn M (1975) Proteins and sodium dodecyl sulfate: Molecular weight determination on polyacrylamide gels and related procedures. In: Neurath H, Hill RL (eds) The proteins, Vol 1, Academic Press, New York, pp 179–223 Winkler H (1976) The composition of adrenal chromaffin granules: An assessment of controversial results. Neuroscience 1:65–80