Abstract
In recent years, there have been enormous advances in the field of protein and peptide engineering and an increased understanding of the way in which biological response modifiers function in the body. It is now possible, through the use of recombinant DNA techniques or by solid phase protein synthesis, to produce on a commercial scale a large variety of regulatory agents that are therapeutically applicable. The list of these response modifiers is continually expanding and includes interferons, interleukins, monoclonal antibodies, colony-stimulating factors, human insulin of recombinant DNA origin, human growth hormones, anticoagulants, and agents that have potential in inflammation and contraception.
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References
Shah, H.K., and Rodgers, R.J. 1990. Biopharmaceutical sales and forecasts. In Spectrum biotechnology overview,March. Little Decision Resources.
Manning, M.C., Patel, K., and Borchardt, R.T. 1989. Stability of protein pharmaceuticals. Pharm. Res. 6: 903–918.
Yoon, J.K., and Burgess, D.J. 1989. Investigation of Interfacial stability of proteins using a surface oscillatory flow technique. Proc. Int. Sym. Control. Release Biact. Mater. 16: 340–341.
Brennan, J.R., Gebhart, S.S.P., and Blackard, W.G. 1985. Pump induced insulin aggregation. A problem with the biostator. Diabetes 34: 353–359.
James, D.E., Jenkins, A.B., Kraegen, E.W., and Chisholm, D.J. 1981. Insulin precipitation in artificial infusion devices. Diabetologia 21: 554–557.
Lougheed, W.D., Woulfe-Flanagan, H., Clement, J.R., and Albisser, A.M. 1980. Insulin aggregation in artificial delivery systems. Diabetologia 19: 1–9.
Peterson, L., Caldwell, J., and Hoffman, J. 1976. Insulin adsorbance to polyvinylchloride surface with implications for constant infusion therapy. Diabetes 25: 7274.
Sefton, M.V. 1982. Implantable micropump for insulin delivery. Effect of a rate controlling membrane. ACS Adv. Chem. Ser. 199: 511–522.
Chawla, A.S., Hinberg, I., Blais, P., and Johnson, D. 1985. Aggregation of insulin containing surfactants, in contact with different materials. Diabetes 34: 420–424.
Iwamoto, G.K., Van Wagenen, R.A., and Andrade, J.D. 1982. Insulin adsorption. Intrinsic tyrosine interfacial fluorescence. J. Colloid Interface Sci. 86: 581–585.
Massey, E.H., and Sheliga, T.A. 1988. Human insulin (HI) isophane suspension (NPH) with improved physical stability. Pharm. Res. 5: S34.
Lougheed, W.D., Albisser, A.M., Martindale, H.M., Chow, J.C., and Clement, J.R. 1983. Physical stability of insulin formulations. Diabetes 32: 424–432.
Sato, S., Ebert, C.D., and Kim, S.W. 1983. Prevention of insulin self-association and self-adsorption. J. Pharm. Sci. 72: 228–232.
Twardowski, Z.J., Nolph, K.D., McGary, T.J., and Moore, H.L. 1983. Influence of temperature and time on insulin adsorption to plastic bags. Am. J. Hosp. Pharm. 40: 583–586.
Twardowski, Z.J., Nolph, K.D., McGary, T.J., Moore, H.L., Collin, P., Ausman, R.K., and Slimack, W.S. 1983. Insulin binding to plastic bags: A methodologic study. Am. J. Hosp. Pharm. 40: 575–579.
Twardowski, Z.J., Nolph, K.D., McGary, T.J., and Moore, H.L. 1983. Nature of insulin binding to plastic bags. Am. J. Hosp. Pharm. 40: 579–581.
Arakawa, T., and Timasheff, S.N. 1984. Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding. Biochemistry 23: 5912–5928.
Arakawa, T., and Timasheff, S.N. 1982. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry 22: 6545–6552.
Ahmad, T., and Bigelow, C.C. 1986. Thermodynamic stability of proteins in salt solutions: A comparison of the effectiveness of protein stabilizers. J. Protein Chem. 5: 355–367.
Bhat, R., and Ahluwalia, J.C. 1985. Effect of calcium chloride on the conformation of proteins. Int. J. Peptide Protein Res. 30: 145–152.
Ahmed, F. 1985. Thermodynamic characterization of the partially denatured states of ribonuclease A in calcium chloride and lithium chloride. Can. J. Biochem. Cell. Biol. 63: 1058–1063.
Almog, R. 1983. Effects of neutral salts on the circular dichroism spectra of ribonuclease A. Biophys. Chem. 17:111–118.
Stellwagen, E., and Babul, J. 1975. Stabilization of the globular structure of ferricytochrome C by chloride in acidic solvents. Biochemistry 14: 5135–5140.
Gekko, K., and Timasheff, S.N. 1981. Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures. Biochemistry 20: 4667–4676.
Gekko, K., and Timasheff, S.N. 1981. Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry 20: 4677–4686.
Lee, J.C., and Timasheff, S.N. 1981. The stabilization of proteins by sucrose. J. Biol. Chem. 256: 7193–7201.
Lee, J.C., and Timasheff, S.N. 1974. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry 13: 257–265.
Lee, J.C., and Timasheff, S.N. 1975. The reconstitution of microtubules from purified calf brain tubulin. Biochemistry 14: 5183–5187.
Bohnert, J.L., and Horbett, T.A. 1986. Changes in adsorbed fibrinogen and albumin interactions with polymers indicated by decreases in detergent elutability. J. Colloid Interface Sci. 3: 363–377.
Piatigorsky, J., Horwitz, J., and Simpson, R.T. 1977. Partial dissociation and renaturation of embryonic chick S-crystallin. Characterization by ultracentrifugation and circular dichroism. Biochim. Biophys. Acta 490: 279–289.
Tandon, S., and Horowitz, P.M. 1987. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effects of the concentration and type of detergent. J. Biol. Chem. 262: 4486–4491.
Robinson, A. B., and Rudd, C.J. 1974. Deamination of Glutaminyl and Asparanginyl Residues in Peptides and Proteins. In Current topics in cellular regulations, Vol. 8. B.L. Horecker and E.R. Stadtman, eds. New York: Academic Press. Pp. 247–295.
Kossiakoff, A.A. 1988. Tertiary structure is a principal determinant to protein deamidation. Science 240: 191–194.
Graf, L., Hajos, G., Patthy, A., and Cseh, G. 1973. The influence of deamidation on the biological activity of porcine adrenocorticotropic hormone (ACTH). Metab. Res. 5: 142–143.
Dixon, H.B. F., Moore, S., Stack-Dunne, M.P., and Young, F.G. 1951. Chromatography of adrenotropic hormone on ion-exchange columns. Nature (London) 168: 1011–1045.
Kuehl, F.A., Jr., Meisinger, M.A.P., Brink, N.G., and Folkers, K. 1953. Pituitary hormones. 6. The purification of corticotropin-ß by counter-current distribution. J. Am. Chem. Soc. 75: 1955–1959.
Rasmussen, H., and Craig, L.C. 1962. 3. Parathyroid hormone. The parathyroid polypeptide. Recent Prog. Horm. Res. 18: 269–295.
Vale, W., Spiess, J., Rivier, C., and Rivier, J. 1981. Characterization of a 41-residue bovine hypothalamic peptide that stimulates secretion of corticotropic and ß-endorphin. Science 213: 1394–1397.
Dedman, M.L., Farmer, T.H., and Morris, C.J.O.R. 1961. Studies on pituitary adrenocorticotrophin. 3. Identification of the oxidation-reduction center. Biochem. J. 78: 348–352.
Riniker, V.B., Neher, R., Maier, R., Kahnt, F.W., Byfield, P.G.H., Gudmundsson, T.V., Galante, L., and MacIntyre, I. 1968. 199. Menschliches calcitonin I. Isolierung and charakterisierung. HeIv. Chem. Acta 51: 1738–1742.
Morley, J.S., Tracey, H.J., and Gregory, R.A. 1965. Structure function relationships in the active C-terminal tetrapeptide sequence of gastrin. Nature (London) 207: 1356–1359.
Jori, G., Galiazzo, G., Marzotto, A., and Scoffone, E. 1968. Dye-sensitized selective photooxidation of methionine. Biochim. Biophys. Acta 154: 1–9.
Kahne, D., and Still, W.C. 1988. Hydrolysis of a peptide bond in neutral water. J. Am. Chem. Soc. 110: 7529–7534.
Ahern, T.J., and Klibanov, A.M. 1985. The mechanism of irreversible enzyme inactivation at 100°C. Science 228: 1280–1284.
Tomlinson, E., and Livingston, C. 1989. Therapeutic peptides and proteins. Pharm. J. 243: 646–648.
Abuchowski, A. 1987. Drug delivery/pharmacokinetics using PEG-modified proteins. J. Cell. Biochem. 11A: 174.
Koziej, P., Mutter, M., Gremlich, H.U., and Holzemann, G. 1985. Conformational studies of synthetic polyethylene glycol bound substance P and its lower analogues. Z. Naturforsch. 40B: 1570–1574.
Mutter, M., Mutter, H., Uhlmann, R., and Bayer, E. 1976. Konformation sumtersuchungen and Oligoalanin, substanz P and der myoglobin sequenz (66–73) der zirkulardichroismus von polyathylenglykol-gebundenen peptiden. Biopolymers 15: 917–927.
Rajasekharan, P.V.N., and Mutter, M. 1981. Conformational studies of poly(oxyethylene)-bound peptides and protein sequences. Acct. Chem. Res. 14: 122–130.
Ribiero, A.A., Saltman, R.P., Goodman, M., and Mutter, M. 1982. ‘H-NMR studies of polyoxyethylene-bound homo-oligo-L-methionines. Biopolymers 21: 2225–2239.
Hashimoto, M., Takada, K., Kiso, Y., and Muanishi, S. 1989. Synthesis of palmitoyl derivatives of insulin and their biological activities. Pharm. Res. 6: 171–176.
Chow, D.D., and Hwang, K.J. 1987. An investigation of the formulation of an insulin-based drug delivery and drug targeting system. J. Pharm. Sci. 76: S49.
Towler, D.A., Eubanks, S.R., Towery, D.S., Adams, S:P., and Glaser, L. 1987. Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase. J. Biol. Chem. 262: 1030–1036.
Ovchinnikov, Y.A., Abdulaev, N.G., and Bogachuk, A.S. 1988. Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated. FEBS Lett. 230: 1–5.
Fojo, A.T., Whitney, P.L., and Awad, M.W., Jr. 1983. Effects of acetylation and guanidination on alkaline conformations of chymotrypsin. Arch. Biochem. Biophys. 224: 636–642.
Gardner, M.L.G. 1984. Intestinal assimilation of intact peptides and proteins from the diet-A neglected field. Biol. Rev. 59: 289–331.
Burger, H.G., and Patel, Y.C. 1977. TSH and TRH: Their physiological regulation and the clinical applications of TRH. In Clinical neuroendocrinology, Chapt. 3. L. Martini and G.M. Besser, eds. New York: Academic Press. Pp. 67–131.
Roger, C.S., Heading, C.E., and Wilkinson, S. 1980. Absorption of two tyrosine containing tetra peptides from the ileum of the rat. IRCS J. Med. Sci. 8: 648.
Hichens, M. 1983. A comparison of thyrotropin-releasing hormone with analogues: Influence of disposition upon pharmacology. Drug Metab. Rev. 14: 77–98.
Yokohama, S., Yamashita, K., Toguchi, H., Takeuchi, J., and Kitamori, N. 1984. Absorption of thyrotropin-releasing hormone after oral administration of TRH tar-tarate monohydrate in the rat, dog and human. J. Pharm. Dyn. 7: 101–111.
Tagesson, C., Anderson, P.A., Anderson, T., Bolin, T., Kallberg, M., and Sjodahl, R. 1983. Passage of molecules through the wall of the gastrointestinal tract; measurement of intestinal permeability to polyethylene glycols in the 634–1338 dalton range (PEG 1000). Scand. J. Gastroenterol 18: 481–486.
Humphrey, M.J., and Ringrose, P.S. 1986. Peptides and related drugs: A review of their absorption, metabolism and excretion. Dr. Metab. Rev. 17 (3, 4): 283–310.
Silk, D.B.A. 1981. Peptide transport. Clin. Sci. 60: 607–615.
Cui, S., Kajiwara, M., Ishii, K., Aoki, K., Sakamoto, J., Matsumiya, T., and Oka, T. 1986. The enhancing effects of amastatin, phosphoramindon and captopril on the potency of [Mets]-enkephalin in rat vas deferens. Japan. J. Pharmcol. 42: 43–49.
Saffran, M., Kumar, G.S., Savariar, C., Burnham, J.C., Williams, F., and Neckers, C.D. 1986. A new approach to the oral administration of insulin and other peptide drugs. Science 233: 1081–1084.
Engel, R.H., and Riggi, S.J. 1969. Intestinal absorption of heparin facilitated by sulfated or sulfonated surfactants. J. Pharm. Sci. 58: 706–710.
Shichiri, M., Yamasaki, Y., Kawamori, R., Kikuchi, M., Hakui, N., and Abe, H. 1978. Increased intestinal absorption of insulin: An insulin suppository. J. Pharm. Pharmacol. 30: 806.
Kidron, M., Eldor, A., Lichtenberg, D., Touitou, E., Ziv, E., and Bar-On, H. 1979. Enteral administration of heparin. Tromb. Res. 16: 833–835.
Kidron, M., Bar-On, H., Berry, E.M., and Ziv, E. 1982. The absorption of insulin from various regions of the rat intestine. Life Sci. 31: 2837.
Ziv, E., Eldor, A., Kleinman, Y., Bar-On, H., and Kidron, M. 1983. Bile salts facilitate the absorption of heparin from the intestine. Biochem. Pharmacol. 32: 773–776.
Ziv, E., Kidron, M., Berry, E.M., and Bar-On, H. 1981. Bile salts promote the absorption of insulin from the rat colon. Life Sci. 29: 803–809.
Ziv, E., Kleinman, Y., Bar-On, H., and Kidron, M. 1984. In Lessons from animal diabetes. E. Shafrier and A.E. Renold, eds. London: Libbey.
Muranishi, S. 1985. Modification of intestinal absorption of drugs by lipoidal adjuvants. Pharm. Res. 2: 108–118.
Kajii, H., Horie, T., Hayashi, M., and Awazu, S. 1985. Fluorescence study on the interaction of salicylate with rat small intestinal epithelial cells: Possible mechanism for promoting effects of salicylate on drug absorption in vivo. Life Sci. 37: 523–530.
Hirai, S., Yasiki, T., Matsuzawa, T., and Mima, H. 1981. Absorption of drugs from the nasal mucosa of rat. Int. J. Pharm. 7: 317–325.
Schanker, L.S., and Johnson, J.M. 1961. Increased Intestinal absorption of foreign organic compounds in the presence of EDTA. Biochem. Pharmacol. 8: 421–422.
Wood, A.J., Maurer, G., Niederberger, W., and Beveridge, T. 1983. Cyclosporine: Pharmacokinetics, metabolism and drug interaction. Transplant. Proc. 15: 2409–2412.
Chemma, M., Palin, K.J., and Davis, S.S. 1987. Lipid vehicles for intestinal lymphatic drug absorption. J. Pharm. Pharmacol. 39: 55–56.
Reymond, J., Sucker, H., and Vonderscher, J. 1988. In vivo model for cyclosporin intestinal absorption in lipid vehicles. Pharm. Res. 5: 677–679.
Teng, C.D. 1989. Studies on some physical and biological properties of compacted protein matrices. Ph.D. thesis, University of Illinois at Chicago.
Killander, D., Dohlwitz, A., Engstedt, L., Franzen, S., Gahrton, G., Gulbring, B., Holm, G., Holmberg, A., Hoglund, S., Killander, A., Lockner, D., Mellstedt, H., Moe, P.J., Palmblad, J., Reizenstein, P., Skarberg, K.O., Swedberg, B., Uden, A.M., Wadman, B., Wide, L., and Ahstrom, L. 1976. Hypersensitive reactions and antibody formation during L-asparaginase treatment of children and adults with acute leukemia. Cancer 37: 220–228.
Langer, R. 1989. Biomaterials in controlled drug delivery: New perspectives from biotechnological advances. Pharm. Tech. 13 (8): 18–30.
Davis, S.S., Ilium, L., McVie, J.G., and Tomlinson, E. 1984. Microspheres and drug therapy. Amsterdam: Elsevier.
Tomlinson, E., and McVie, J.G. 1983. New directions in cancer chemotherapy 2. Targeting with microspheres. Pharm. Ind. 281–284.
Ilium, L. and Davis, S.S. 1982. The targeting of drugs parenterally by use of microspheres. J. Parent. Sci. Technol. 36: 242–248.
Ballanti, J.A. 1985. Immunology III. Philadelphia: Saunders.
Ilium, L., Jones, P.D.E., and Davis, S.S. 1984. Drug targeting using monoclonal antibody-coated nanoparticles. In Microspheres and drug therapy: Pharmaceutical, immunological and medical aspects. S.S. Davis, L. Ilium, J.G. McVie, and E. Tomlinson, eds. Amsterdam: Elsevier. Pp. 353–363.
DeDuve, C., DeBarsay, T., Poole, B., Trouet, A., Tulkens, P., and van Hoof, F. 1974. Commentary, Lysosomotropic agents. Biochem. Pharmacol. 23: 2495–2531.
Fidler, I.J. 1980. Therapy of spontaneous metastases by intravenous injection of liposomes containing lymphokines. Science 208: 1469–1471.
Baldwin, R.W., and Garnet, M.C. 1955. Monoclonal antibodies for cancer detection and therapy. London: Academic Press.
Trouet, A., Deprez-De Compeneere, D., and DeDuve, C. 1972. Chemotherapy through lysosomes with a DNA-Daunorubicin complex. Nature (New Biol.) 239: 110–112.
Ghitescu, L., Fixman, A., Simionescu, M., and Simionescu, N. 1986. Specific binding sites for albumin restricted to plasmalemmal vesicles of continuous capillary endothelium: Receptor-medicated trranscytosis. J. Biol. Chem. 102: 1304–1311.
Kopecek, J., and Duncan, R. 1987. Poly[N-(2-hydroxypropyl)-methacrylamide] macromolecules as drug carrier systems. In Polymers in controlled drug delivery. L. Ilium and S.S. Davis, eds. Bristol, U.K.: Wright. Pp. 152–187.
Szoka, F.J., and Paphadjopoulas, D. 1980. Comparative properties and methods of preparation of lipid vesicles (liposomes). Annu. Rev. Biophys. Bioeng. 9: 467–508.
Godfredsen, C.F., Van Berkel, Th.J.C., Kruijt, J.K., and Goethais, A. 1983. Cellular localization of stable solid liposomes in the liver of rats. Biochem. Pharmacol. 32: 3389–3396.
Ostro, M.J. 1983. Liposomes. New York: Dekker.
Burgess, D.J., and Carless, J.E. 1985. Manufacture of gelatin/gelatin coacervate microcapsules. Int. J. Pharm. 27: 61–70.
Burgess, D.J., Davis, S.S., and Tomlinson, E. 1987. Potential use of albumin microspheres as a drug delivery system. 1. Preparation and in vitro release of steroids. Int. J. Pharm. 39: 129–136.
Widder, K., Flouret, G., and Senyei, A. 1979. Magnetic microspheres: Synthesis of a novel parenteral drug carrier. J. Pharm. Sci. 68: 79–82.
Oppenheim, R.C. 1981. Solid colloidal drug delivery systems: Nanoparticles, Int. J. Pharm. 8: 217–234.
Birrenback, G., and Speiser, F. 1976. Polymerized micelles and their use as adjuvants. J. Pharm. Sci. 65: 1763–1766.
Couvreur, P., Kante, B., Roland, M., Guiot, P., Bauduin, P., and Speiser, P. 1979. Polycyanoacrylate nanocapsules as potential lysosomotropic carriers: Preparation, morphological and sorptive properties. J. Pharm. Pharmacol. 31: 331–332.
Schoeft, G.1., and French J.E. 1968. Vacular permeability to particulate fat: Morphological observations on vessels of lactating mammary gland and of lung. Proc. Roy. Soc. London [Biol.] 169: 153–165.
Wilson, G. 1986. Genes therapy: Rationale and realization. In Site-specific drug delivery. E. Tomlinson and S.S. Davis, eds. Chichester, U.K.: Wiley. Pp. 149–164.
Karlson, S., Humphries, R.K., Gluzman, Y., and Nienhuis, A.W. 1985. Transfer of genes into hematopoietic cells using recombinant DNA viruses. Proc. Natl. Acad. Sci. U.S.A. 82: 158–162.
Gallo, J.M., Hung, C.T., and Perrier, D.G. 1983. Analysis in albumin microsphere preparation. Int. J. Pharm. 22: 63–74.
Waser, P.G., Muller, V., Krueuter, J., Berger, S., Munz, K., Kaiser, E., and Pfluger, B. 1987. Localization of colloidal particles (liposomes, hexyclyanoacrylate nanoparticles and albumin nanoparticles) by histology and autoradiography in mice. Int. J. Pharm. 39: 213–227.
Royer, G.P., Lee, T.K., and Sokoloski, T.D. 1983. Entrapment of bioactive compounds within native albumin beads. J. Parenteral Sci. Technol. 37 (2): 34–37.
Ihler, G.M. 1986. Methods of drug delivery. New York: Pergamon.
Kwok, K.K., Groves, M.J., and Burgess, D.J. 1989. Sterile microencapsulation of BCG in alginate-poly(1-lysine) by an air spraying technique. Proc. Int. Sym. Control. Release Bioact. Mater. 16: 242–342.
Schakenraad, J., Oosterbaan, J., Nieuwenhuis, P., Molenaar, I., Olojslager, J., Potman, W., Eenink, M., and Feijen, J. 1988. Biodegradable hollow fibers for the controlled release of drugs. Biomaterials 9: 116–120.
Hsieh, D.S.T., Langer, R., and Folkman, J. 1981. Magnetic modulation of release of macromolecules from polymers. Proc. Natl. Acad. Sci. U.S.A. 78: 1863–1867.
Guy, R.H., and Hadgraft, J. 1988. Physicochemical aspects of percutaneous penetration and its enhancement. Pharm. Res. 5 (12): 753–758.
Chien, Y.W., Siddiqui, O., Sun, Y., Shi, W.M., and Liu, J.C. 1987. Transdermal inotphoretic delivery of therapeutic peptides/proteins. 1. Insulin. Ann. N.Y. Acad. Sci. 507: 32–51.
Burnette, R.R., and Marrero, D. 1986. Comparison between the iontrophoretic transparent of thyrotropin releasing hormone across excised nude mouse skin. J. Pharm. Sci. 75: 738–743.
Nanavaty, M., Brucks, R., Grimes, H., and Siegel, F.P. 1989. An ATR-FTIR approach to study the effect of ultrasound on human skin. Proc. Int. Sym. Control. Release Bioact. Mater. 16: 310–311.
Golden, G.M., Guzek, D.B., Kennedy, A.H., and Potts, R.P. 1987. Stratum corneum lipid phase transitions and water barrier properties. Biochemistry 26: 2382–2388.
Su, K.S.E. 1986. Intranasal delivery of peptides and proteins. Pharm. Int. 7: 8–11.
Su, K.S.E., Campanale, K.M., Medelsohn, L.G., Kerschner, G.A., and Gries, C.L. 1985. Nasal delivery of polypeptides. 1. Nasal absorption of enkephalins in rats. J. Pharm. Sci. 74: 394–398.
Hanson, M., Gazdick, G., Cahill, J., and Augustine, M. 1986. Intranasal delivery of the peptide salmon calcitonin. In Delivery systems for peptide drugs. S.S. Davis, L. Ilium, and E. Tomlinson, eds. New York: Plennum. Pp. 233–242.
Sandow, J., and Petri, W. 1985. Intranasal administration of peptides. Biological activity and therapeutic efficacy. In Transnasal systemic medications. Y.W. Chien, Ed. Amsterdam: Elsevier. Pp. 183–199.
Gordon, G.S., Moses, A.C., Silver, R.D., Flier, J.S., and Carey, M.C. 1985. Nasal absorption of insulin: Enhancement by hydrophobic slats. Proc. Natl. Acad. Sci. U.S.A. 82: 7419–7423.
Davies, H.W., Scott, G.M., Robinson, J.A., Higgins, P.G., Wootton, R., and Tyrrell, D.A.J. 1983. Comparative intranasal pharmacokinetics of interferon using 2 spray systems. J. Interferon Res. 3: 443–449.
Stratford, R.E., Jr., and Lee, V.H. L. 1986. Aminopeptidase activity in homogenates of various absorptive mucosae in the albino rabbit: Implications of peptide delivery. Int. J. Pharm. 30: 73–82.
Nishihata, T., Rytting, J.H. Higuchi, T., and Caldwell, L. 1981. Enhanced rectal absorption of insulin and heparin in rats in the presence of nonsurfactant adjuvants. J. Pharm. Sci. 33: 334–335.
Wespi, H.J., and Rehsteiner, H.P. 1966. Erfahrungen mit Syntocinon und ODABuccaltabletten. Gynaecologia 162: 414–418.
Chang, H.S., Park, H., Kelly, P., and Robinson, J.R. 1985. Bioadhesive polymers as platforms for oral controlled drug delivery. 2. Synthesis and evaluation of some swelling water-insoluble bioadhesive polymers. J. Pharm. Sci. 74: 399–405.
Park, H., and Robinson, J.R. 1986. Physico-chemical properties of water insoluble polymers important to mucin/epithelial adhesion. In Advances in drug delivery systems. J.M. Anderson and S.W. Kim, eds. Amsterdam: Elsevier. Pp. 47–60.
Peppas, N.A., and Buri, P.A. 1986. Surface interfacial and molecular aspects of polymer bioadhesion on soft tissues. In Advances in drug delivery systems. J.M. Anderson and S.W. Kim, eds. Amsterdam: Elsevier. Pp. 257–265.
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Burgess, D.J. (1993). Drug Delivery Aspects of Biotechnology Products. In: Pezzuto, J.M., Johnson, M.E., Manasse, H.R. (eds) Biotechnology and Pharmacy. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-8135-6_6
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